MIRA
INFORM REPORT
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Report Date : |
23.08.2011 |
IDENTIFICATION DETAILS
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Name : |
MG2 SRL |
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Registered Office : |
Via Del Savena 18 Pian Di Macina Pianoro, 40065 |
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Country : |
Italy |
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Financials (as on) : |
31.12.2009 |
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Date of Incorporation : |
19.11.1997 |
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Com. Reg. No.: |
01819491208 |
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Legal Form : |
Private Subsidiary |
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Line of Business : |
Manufacture of other special purpose machinery not elsewhere classified |
RATING & COMMENTS
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MIRA’s Rating : |
B |
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RATING |
STATUS |
PROPOSED CREDIT LINE |
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26-40 |
B |
Capability to overcome financial difficulties seems comparatively
below average. |
Small |
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Status : |
Moderate |
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Payment Behaviour : |
Satisfactory |
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Litigation : |
Clear |
NOTES :
Any query related to this report can be made on
e-mail: infodept@mirainform.com
while quoting report number, name and date.
ECGC Country Risk Classification List – March 31st, 2011
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Country Name |
Previous Rating (31.12.2010) |
Current Rating (31.03.2011) |
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Italy |
A2 |
A2 |
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Risk Category |
ECGC
Classification |
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Insignificant |
A1 |
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Low |
A2 |
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Moderate |
B1 |
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High |
B2 |
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Very High |
C1 |
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Restricted |
C2 |
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Off-credit |
D |
Company name and address
Mg2 SRL
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Business
Description
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Mg2 SRL is primarily engaged in manufacture of machinery for working soft
rubber or plastics or for the manufacture of products of these materials
(extruders, moulders, pneumatic tyre making or retreading machines and other
machines for making a specific rubber or plastic product); manufacture of
printing and bookbinding machines; manufacture of machinery for producing
tiles, bricks, shaped ceramic pastes, pipes, graphite electrodes, blackboard
chalk, foundry moulds, etc.; manufacture of moulding boxes for any material;
mould bases; moulding patterns; moulds; manufacture of dryers for wood, paper
pulp, paper or paperboard; manufacture of centrifugal clothes dryers;
manufacture of diverse special machinery and equipment (machines to assemble
electric or electronic lamps, tubes (valves) or bulbs; machines for
production or hot-working of glass or glassware, glass fibre or yarn;
machinery or apparatus for isotopic separation; rope-making machinery, etc.);
and manufacture of industrial robots for multiple uses. |
Industry
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Industry |
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ANZSIC 2006: |
2499 - Other Machinery and Equipment Manufacturing
Not Elsewhere Classified |
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NACE 2002: |
2956 - Manufacture of other special purpose
machinery not elsewhere classified |
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NAICS 2002: |
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UK SIC 2003: |
2956 - Manufacture of other special purpose
machinery not elsewhere classified |
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US SIC 1987: |
Key
Executives
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News
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1 - Profit & Loss Item Exchange Rate: USD 1 = EUR 0.7190468
2 - Balance Sheet Item Exchange Rate: USD 1 = EUR 0.6969855
Corporate Overview
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Corporate Structure News
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H.P.F. SRL |
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Mg2 SRL |
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Company Name |
Company Type |
Location |
Country |
Industry |
Sales |
Employees |
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Parent |
Pianoro, Bologna |
Italy |
Commercial Banks |
1.4 |
1 |
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Subsidiary |
Pianoro, Bologna |
Italy |
Miscellaneous Capital Goods |
27.9 |
180 |
Executives Report
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Scientists at Columbia University Report Research in Coenzymes |
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Coenzymes |
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Health &
Medicine Week |
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[What follows is
the full text of the news story.] "Biotin
carboxylase (BC) activity is shared among biotin-dependent carboxylases and catalyzes
the Mg-ATP-dependent carboxylation of biotin using bicarbonate as the CO2
donor. BC has been studied extensively over the years by structural, kinetic,
and mutagenesis analyses," scientists writing in the Journal of
Biological Chemistry report (see also Coenzymes). "Here we
report three new crystal structures of Escherichia coli BC at up to 1.9
angstrom resolution, complexed with different ligands. Two structures are
wild-type BC in complex with two ADP molecules and two Ca2+ ions or two ADP
molecules and one Mg2+ ion. One ADP molecule is in the position normally
taken by the ATP substrate, whereas the other ADP molecule occupies the
binding sites of bicarbonate and biotin. One Ca2+ ion and the Mg2+ ion are
associated with the ADP molecule in the active site, and the other Ca2+ ion
is coordinated by Glu-87, Glu-288, and Asn-290. Our kinetic studies confirm
that ATP shows substrate inhibition and that this inhibition is competitive against
bicarbonate. The third structure is on the R16E mutant in complex with
bicarbonate and Mg-ADP. Arg-16 is located near the dimer interface. The R16E
mutant has only a 2-fold loss in catalytic activity compared with the
wild-type enzyme. Analytical ultracentrifugation experiments showed that the
mutation significantly destabilized the dimer, although the presence of
substrates can induce dimer formation. The binding modes of bicarbonate and
Mg-ADP are essentially the same as those to the wild-type enzyme. However,
the mutation greatly disrupted the dimer interface and caused a large
re-organization of the dimer," wrote C.Y. Chou and colleagues, Columbia
University. The researchers
concluded: "The structures of these new complexes have implications for the
catalysis by BC." Chou and
colleagues published their study in the Journal of Biological Chemistry
(Structural and Biochemical Studies on the Regulation of Biotin Carboxylase
by Substrate Inhibition and Dimerization. Journal of Biological Chemistry, 2011;286(27):24417-24425). Additional
information can be obtained by contacting L. Tong, Columbia University, Dept.
of Biology Science, New York City, NY 10027, United States. The publisher of
the Journal of Biological Chemistry can be contacted at: American Society
Biochemistry Molecular Biology Inc., 9650 Rockville Pike, Bethesda, MD
20814-3996, USA. |
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Researchers from National Institutes of Health Report Details of New
Studies and Findings in the Area of Life Science |
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Life Science |
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Health &
Medicine Week |
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[What follows is
the full text of the news story.] According to the
authors of recent research from Bethesda, Maryland, "The magnesium ion, Mg2+,
is essential for all life as a cofactor for ATP, polyphosphates such as DNA
and RNA, and metabolic enzymes, but whether it plays a part in intracellular
signalling (as Ca2+ does) is unknown. Here we identify mutations in the
magnesium transporter gene, MAGT1, in a novel X-linked human immunodeficiency
characterized by CD4 lymphopenia, severe chronic viral infections, and
defective T-lymphocyte activation." "We
demonstrate that a rapid transient Mg2+ influx is induced by antigen receptor
stimulation in normal T cells and by growth factor stimulation in
non-lymphoid cells. MAGT1 deficiency abrogates the Mg2+ influx, leading to
impaired responses to antigen receptor engagement, including defective
activation of phospholipase C gamma 1 and a markedly impaired Ca2+ influx in
T cells but not B cells," wrote F.Y. Li and colleagues, National
Institutes of Health (see also Life Science). The researchers
concluded: "These observations reveal a role for Mg2+ as an
intracellular second messenger coupling cell-surface receptor activation to
intracellular effectors and identify MAGT1 as a possible target for novel
therapeutics." Li and
colleagues published their study in Nature (Second messenger role for Mg2+
revealed by human T-cell immunodeficiency. Nature, 2011;475(7537):471-U63). For additional
information, contact F.Y. Li, NIAID, Molecular Development Sect, Lymphocyte
Molecular Genetics Unit, Immunology Laboratory, National Institutes of
Health, Bethesda, MD 20892, United States. Publisher
contact information for the journal Nature is: Nature Publishing Group,
Macmillan Building, 4 Crinan St., London N1 9XW, England. |
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Studies in the Area of Enzymes and Coenzymes Reported from University
of Jinan |
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Enzymes and Coenzymes |
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Life Science
Weekly |
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[What follows is
the full text of the news story.] "A novel
glycoside hydrolases family 57 gene (gh-57) was found from a metagenomic fosmid
library constructed from a black smoker chimney sample 4143-1 from the Mothra
hydrothermal vent at the Juan de Fuca Ridge. Sequence and homology analysis
using BLAST revealed that it had high similarity to gh-57 family,"
investigators in Guangdong, People's Republic of China report (see also Enzymes and Coenzymes). "Conserved
domain research revealed that the novel gh-57 contained a Glyco-hydro-57
domain and five conserved regions, including two putative catalytic residues
Glu(154) and Asp(263). The three-dimensional features of the protein and its
homologue from Pyrococcus horikoshii OT3 known as alpha-amylase were
generated by homology modeling. The gh-57 gene was cloned, expressed, and
purified in Escherichia coli using pQE system. Enzyme activity revealed that
the recombinant protein could hydrolyze soluble starch and demonstrated
amylase activity. It showed an optimal pH of 7.5, an optimal temperature of
90A degrees C, and its thermostability at 90A degrees C could remain over 50%
enzyme activity for 4 h. The enzyme activity could be increased by DTT and
Mg2+ while an inhibitory effect was observed with EDTA, ATP, and Ca2+,"
wrote H. Wang and colleagues, University of Jinan. The researchers
concluded: "These results showed that the gh-57 gene was a novel
thermostable amylase from oceanic microorganisms." Wang and
colleagues published their study in Applied Biochemistry and Biotechnology (Identification
and Characterization of a Novel Thermostable gh-57 Gene from Metagenomic
Fosmid Library of the Juan De Fuca Ridge Hydrothemal Vent. Applied
Biochemistry and Biotechnology, 2011;164(8):1323-1338). For additional
information, contact Z.H. Liu, Jinan University, Research Center Molecular
Biology, College Life Science & Technology, Institute Life & Health
Engineering, National Engineering & Research Center Genetics Medical,
Guangzhou 510632, Guangdong, People's Republic of China. The publisher of
the journal Applied Biochemistry and Biotechnology can be contacted at:
Humana Press Inc., 999 Riverview Drive Suite 208, Totowa, NJ 07512, USA. |
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New Data from Mayville State University Illuminate Research in Enzymes
and Coenzymes |
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Enzymes and Coenzymes |
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Life Science
Weekly |
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[What follows is
the full text of the news story.] "Aldehyde
dehydrogenase 2 (ALDH2) catalyzes oxidation of toxic aldehydes to carboxylic acids.
Physiologic levels of Mg2+ ions influence ALDH2 activity in part by
increasing NADH binding affinity," scientists in Mayville, North Dakota
report (see also Enzymes and Coenzymes). "Traditional
fluorescence measurements monitor the blue shift of the NADH fluorescence
spectrum to study ALDH2-NADH interactions. By using time-resolved
fluorescence spectroscopy, we have resolved the fluorescent lifetimes (tau)
of free NADH (tau = 0.4 ns) and bound NADH (tau = 6.0 ns). We used this
technique to investigate the effects of Mg2+ on the ALDH2-NADH binding
characteristics and enzyme catalysis. From the resolved free and bound NADH
fluorescence signatures, the K-D for NADH with ALDH2 ranged from 468 to 12 mc
M for Mg2+ ion concentrations of 20 to 6000 mc M, respectively. The rate
constant for dissociation of the enzyme-NADH complex ranged from 0.4s(-1)
(6000 mc M Mg2+) to 8.3 s(-1) (0 mc M Mg2+) as determined by addition of
excess NAD(+) to prevent re-association of NADH and resolving the real-time
NADH fluorescence signal. The apparent NADH association/re-association rate
constants were approximately 0.04 mu M-1 s(-1) over the entire Mg2+ ion
concentration range and demonstrate that Mg2+ ions slow the release of NADH
from the enzyme rather than promoting its re-association. We applied NADH
fluorescence lifetime analysis to the study of NADH binding during enzyme
catalysis. Our fluorescence lifetime analysis confirmed complex behavior of
the enzyme activity as a function of Mg2+ concentration. Importantly, we
observed no pre-steady state burst of NADH formation," wrote T.P.
Gonnella and colleagues, Mayville State University. The researchers
concluded: "Furthermore, we observed distinct fluorescence signatures
from multiple ALDH2-NADH complexes corresponding to free NADH, enzyme-bound
NADH, and, potentially, an abortive NADH-enzyme-propanal complex (tau =
11." Gonnella and
colleagues published their study in Chemico - Biological Interactions (NADH
fluorescence lifetime analysis of the effect of magnesium ions on ALDH2.
Chemico - Biological Interactions, 2011;191(1-3 Sp. Is):147-152). For more
information, contact T.P. Gonnella, Mayville State University, Division
Science & Math, 330 3rd St. NE, Mayville, ND 58257, United States. Publisher
contact information for the journal Chemico - Biological Interactions is:
Elsevier Ireland Ltd., Elsevier House, Brookvale Plaza, East Park Shannon,
Co. Clare, Ireland. |
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Findings from University of Waterloo Broaden Understanding of
Molecular Biosystems |
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Molecular Biosystems |
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Life Science
Weekly |
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[What follows is
the full text of the news story.] According to the
authors of a study from Waterloo, Canada, "The binding of small molecule
targets by RNA aptamers provides an excellent model to study the versatility
of RNA function. The malachite green aptamer binds and recognizes its ligand
via stacking and electrostatic interactions." "The
binding of the aptamer to its original selection target and three related
molecules was determined by isothermal titration calorimetry, equilibrium
dialysis, and fluorescence titration. The results reveal that the entropy of
complex formation plays a large role in determining binding affinity and
ligand specificity," wrote J.B. Dacosta and colleagues, University of
Waterloo (see also Molecular Biosystems). The researchers
concluded: "These data combined with previous structural studies show
that metal ions are required to stabilize the complexes with non-native
ligands whereas the complex with the original selection target is stable at
low salt and in the absence of divalent metal ions." Dacosta and
colleagues published their study in Molecular Biosystems (Entropy and Mg2+
control ligand affinity and specificity in the malachite green binding RNA
aptamer. Molecular Biosystems, 2011;7(7):2156-2163). For more information,
contact T. Dieckmann, University of Waterloo, Dept. of Chemical, 200
University Avenue W, Waterloo, ON N2L 3G1, CANADA. Publisher
contact information for the journal Molecular Biosystems is: Royal Society
Chemistry, Thomas Graham House, Science Park, Milton Rd., Cambridge CB4 0WF,
Cambs, England. |
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Research Data from R.W. Lucas and Colleagues Update Understanding of
Nitrogen |
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Nitrogen |
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Ecology,
Environment & Conservation |
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[What follows is
the full text of the news story.] According to the
authors of a study from Umea, Sweden, "The dominant base cations (BC:
i.e., Ca2+, Mg2+, K+, and Na+) are important in buffering soil and water
acidity in both terrestrial and aquatic ecosystems. Ca2+., Mg2+, and K+ are
also important in many plant physiological functions." "Because BC
availability is affected by changes in the nitrogen (N) cycle, we conducted a
meta-analysis of previously published data to determine if N fertilization
alters the availability of BC in terrestrial and stream ecosystems across
biomes. We include data from 107 independent studies published in 62
different articles, taking a holistic perspective on BC by examining their
responses to added N in plant foliage, bulk soil, soil solution, and stream
water. Our results suggest N fertilization may accelerate BC loss from
terrestrial ecosystems over time periods less than five years. We found that
N additions resulted in an overall 24% decrease in the availability of
exchangeable Ca2+, Mg2+, and K+ in the bulk soil of boreal forest, temperate
forest, and grassland biomes. Collectively, responses of BC in boreal forest,
temperate forest, tropical forest, and grassland biomes increased following N
fertilization by about 71% in soil solution and 48% in stream waters.
Additionally, BC responses in foliage decreased in boreal forest and
temperate forest biomes following N additions over time periods less than
five years, but there were no significant changes over longer time periods.
Despite large short-term shifts in BC responses following N additions, we did
not find evidence of widespread negative impacts on ecosystems over time
periods greater than five years. This analysis suggests effects of N addition
on the availability of exchangeable BC may diminish over time," wrote
R.W. Lucas and colleagues. The researchers
concluded: "Although the effects on BC can be substantial over periods
less than five years, there is little available evidence that N fertilization
has had large-scale detrimental effects on the availability of BC needed for
plant growth within terrestrial or aquatic ecosystems." Lucas and
colleagues published the results of their research in Forest Ecology and
Management (A meta-analysis of the effects of nitrogen additions on base
cations: Implications for plants, soils, and streams. Forest Ecology and
Management, 2011;262(2):95-104). For additional
information, contact R.W. Lucas, SLU Swedish University Agriculture Science,
Dept. of Forest Ecology & Management, 17 Linneaus Vagan, SE-90183 Umea,
SWEDEN. The publisher of
the journal Forest Ecology and Management can be contacted at: Elsevier
Science BV, PO Box 211, 1000 AE Amsterdam, Netherlands. |
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Research from University of Shandong Reveals New Findings on Anions |
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Anions |
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Global Warming
Focus |
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[What follows is
the full text of the news story.] "In this
work, the possibility of achieving fixation of CO2 using Ca and Mg ions was tested
and verified. Concentrated seawater from desalination plants, subsurface
brines, industrial effluents with high hardness, and/or natural seawaters
that are rich in Ca2+ and Mg2+ could all be potential aqueous sources,"
scientists in Jinan, People's Republic of China report. "Theoretical
analyses indicated that the carbonation reaction could be enhanced by raising
the pH or the CO2 partial pressure. Experiments using synthesized seawater
confirmed this possibility. Over 90% of the Ca2+ and Mg2+ ions in the
seawater could be converted by precipitation in the forms of MgCO3 and
dolomite [MgCa(CO3)(2)], and the kinetics of the process was found to be
quite acceptable. It was found that 1 m(3) of natural seawater could fix
about 1.34 m(3) or 2.65 kg of CO2 (gas volume, standard conditions), and the
potential of concentrated seawater is 2-3 times this value. Even if the
annual CO2 emissions of the entire world were captured in this way, the
concentration of Ca2+/Mg2+ in natural seawater would change at only the
part-per-million scale, such that the ecological effects could be negligible.
This idea has great potential for application," wrote W.L. Wang and
colleagues, University of Shandong. The researchers
concluded: "It might be able to realize not only the permanent fixation
of CO2 but also the production of large amounts of carbonate
byproducts." Wang and
colleagues published their study in Industrial & Engineering Chemistry
Research (CO2 Fixation in Ca2+-/Mg2+-Rich Aqueous Solutions through Enhanced
Carbonate Precipitation. Industrial & Engineering Chemistry Research,
2011;50(13):8333-8339). For additional
information, contact W.L. Wang, Shandong University, National Engineering
Laboratory Coal Fired Pollutants Emiss Reduct, Jinan 250061, People's
Republic of China. The publisher's
contact information for the journal Industrial & Engineering Chemistry
Research is: American Chemical Society, 1155 16th St., NW, Washington, DC
20036, USA. |
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Studies from University of British Columbia Describe New Findings in
Porphyrins |
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Porphyrins |
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Life Science
Weekly |
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[What follows is
the full text of the news story.] "Heme and bacteriochlorophyll
a (BChl) biosyntheses share the same pathway to protoporphyrin IX, which then
branches as follows. Fe2+ chelation into the macrocycle by ferrochelatase
results in heme formation, and Mg2+ addition by Mg-chelatase commits the
porphyrin to BChl synthesis," researchers in Vancouver, Canada report
(see also Porphyrins). "It was
recently discovered that a bchD (Mg-chelatase) mutant of Rhodobacter
sphaeroides produces an alternative BChl in which Mg2+ is substituted by
Zn2+. Zn-BChl has been found in only one other organism before, the
acidophilic Acidiphilium rubrum. Our objectives in this work on the bchD
mutant were to 1) elucidate the Zn-BChl biosynthetic pathway in this organism
and 2) understand causes for the low amounts of Zn-BChl produced. The bchD
mutant was found to contain a Zn-protoporphyrin IX pool, analogous to the
Mg-protoporphyrin IX pool found in the wild type strain. Inhibition of
ferrochelatase with N-methylprotoporphyrin IX caused Zn-protoporphyrin IX and
Zn-BChl levels to decline by 80-90% in the bchD mutant, whereas in the wild
type strain, Mg-protoporphyrin IX and Mg-BChl levels increased by 170-240%.
Two early metabolites of the Zn-BChl pathway were isolated from the bchD
mutant and identified as Zn-protoporphyrin IX monomethyl ester and
divinyl-Zn-protochlorophyllide. Our data support a model in which
ferrochelatase synthesizes Zn-protoporphyrin IX, and this metabolite is acted
on by enzymes of the BChl pathway to produce Zn-BChl," wrote P.R.
Jaschke and colleagues, University of British Columbia. The researchers
concluded: "Finally, the low amounts of Zn-BChl in the bchD mutant may
be due, at least in part, to a bottleneck upstream of the step where divinyl-Zn-protochlorophyllide
is converted to monovinyl-Zn-protochlorophyllide." Jaschke and
colleagues published their study in the Journal of Biological Chemistry (A
bchD (Magnesium Chelatase) Mutant of Rhodobacter sphaeroides Synthesizes Zinc
Bacteriochlorophyll through Novel Zinc-containing Intermediates. Journal of
Biological Chemistry, 2011;286(23):20313-20322). For additional
information, contact J.T. Beatty, University of British Columbia, Dept. of
Microbiology & Immunology, 2350 Health Science Mall, Vancouver, BC V6T
1Z3, CANADA. Publisher
contact information for the Journal of Biological Chemistry is: American
Society Biochemistry Molecular Biology Inc., 9650 Rockville Pike, Bethesda,
MD 20814-3996, USA. |
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Researchers from Zhejiang University Discuss Findings in Electrolytes |
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Electrolytes |
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Life Science
Weekly |
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[What follows is
the full text of the news story.] According to the
authors of recent research from Zhejiang, People's Republic of China, "Glycogen
synthase kinase 3 beta (GSK3 beta) is a serine/threonine kinase that requires
two cofactor Mg2+ ions for catalysis in regulating many important cellular
signals. Experimentally, Li+ is a competitive inhibitor of GSK3 beta relative
to Mg2+, while this mechanism is not experienced with other group I metal
ions." "Herein, we
use native Mg-2(2+)-Mg-1(2+) GSK3 beta and its Mg-2(2+)-M-1(+) (M = Li, Na,
K, and Rb) derivatives to investigate the effect of metal ion substitution on
the mechanism of inhibition through two-layer ONIOM-based quantum
mechanics/molecular mechanics (QM/MM) calculations and molecular dynamics
(MD) simulations. The results of ONIOM calculations elucidate that the
interaction of Na+, K+, and Rb+ with ATP is weaker compared to that of Mg2+
and Li+ with ATP, and the critical triphosphate moiety of ATP undergoes a
large conformational change in the Na+, K+, and Rb+ substituted systems. As a
result, the three metal ions (Na+, K+, and Rb+) are not stable and depart
from the active site, while Mg2+ and Li+ can stabilize in the active site,
evident in MD simulations. Comparisons of Mg-2(2+)-Mg-1(2+) and
Mg-2(2+)-Li-1(+) systems reveal that the inline phosphor-transfer of ATP and
the two conserved hydrogen bonds between Lys85 and ATP, together with the
electrostatic potential at the Li-1(+) site, are disrupted in the
Mg-2(2+)-Li-1(+) system," wrote S.Y. Lu and colleagues, Zhejiang
University (see also Electrolytes). The researchers
concluded: "These computational results highlight the possible mechanism
why Li+ inhibits GSK3 beta." Lu and
colleagues published their study in Physical Chemistry Chemical Physics
(Dissection of the difference between the group I metal ions in inhibiting
GSK3 beta: a computational study. Physical Chemistry Chemical Physics,
2011;13(15):6983-6992). For additional
information, contact Y.J. Jiang, Zhejiang University, Ningbo Institute
Technology, Key Laboratory Molecular Design & Nutrition Engineering,
Ningbo 315104, Zhejiang, People's Republic of China. Publisher
contact information for the journal Physical Chemistry Chemical Physics is:
Royal Society Chemistry, Thomas Graham House, Science Park, Milton Rd.,
Cambridge CB4 0WF, Cambs, England. |
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Researchers from Case Western Reserve University Discuss Findings in
Life Science |
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Life Science |
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Health &
Medicine Week |
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[What follows is
the full text of the news story.] Researchers
detail in "Cation selectivity by the CorA Mg2+ channel requires a fully
hydrated cation," new data in Life Science. "The CorA Mg(2+)
channel is the primary uptake system in about half of all bacteria and
archaea. However, the basis for its Mg(2+) selectivity is unknown,"
investigators in Cleveland, Ohio report (see also Life Science). "Previous
data suggested that CorA binds a fully hydrated Mg(2+) ion, unlike other ion
channels. The crystal structure of Thermotoga maritima CorA shows a
homopentamer with two transmembrane segments per monomer connected by a short
periplasmic loop. This highly conserved loop, (281)EFMPELKWS(289) in
Salmonella enterica serovar Typhimurium CorA, is the only portion of the
channel outside of the cell, suggesting a role in cation selectivity.
Mutation of charged residues in the loop, E281 and K287, to any of several
amino acids had little effect, demonstrating that despite conservation
electrostatic interactions with these residues are not essential. While
mutation of the universally conserved E285 gave a minimally functional
channel, E285A and E285K mutants were the most functional, again indicating
that the negative charge at this position is not a determining factor. Several
mutations at K287 and W288 behaved anomalously in a transport assay. Analysis
indicated that mutation of K287 and W288 disrupts cooperative interactions
between distinct Mg(2+) binding sites. Overall, these results are not
compatible with electrostatic interaction of the Mg(2+) ion with the
periplasmic loop. Instead, the loop appears to form an initial binding site
for hydrated Mg(2+), not for the dehydrated cation," wrote A.S. Moomaw
and colleagues, Case Western Reserve University. The researchers concluded:
"The loop residues may function to accelerate dehydration of the before
entry of Mg(2+) into the pore of the channel." Moomaw and
colleagues published their study in Biochemistry (Cation selectivity by the
CorA Mg2+ channel requires a fully hydrated cation. Biochemistry,
2010;49(29):5998-6008). For additional
information, contact A.S. Moomaw, Dept. of Pharmacology, School of Medicine,
Case Western Reserve University, Cleveland Ohio 44106-4965, United States. The publisher of
the journal Biochemistry can be contacted at: Springer, 233 Spring Street,
New York, NY 10013, USA. |
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MG2 S.r.l. Files Patent Application for Machine for Filling Containers
with at least One Product |
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Indian Patent
News |
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[What follows is
the full text of the article.] New Delhi, Sept.
6 -- Italy based MG2 S.r.l. filed patent application for machine for filling
containers with at least one product. The inventor is Angelo Ansaloni. MG2 S.r.l. filed
the patent application on Feb. 17, 2009. The patent application number is
300/DEL/2009 A. The international classification number is A47F1/035. According to the
Controller General of Patents, Designs & Trade Marks, "On a
continuous machine for filling containers with at least one product, each
container is fed along a given path in time with a relative metering device
which withdraws the product from a tank feeds the withdrawn product into the
container and has a piston and a cylinder movable axially with respect to
each other; and a lock device provides for selectively locking the pistons
and relative cylinders." MG2 was founded
in 1966, when it introduced the first continuous-motion capsule filler on the
market-model G36. Since then MG2 has supplied thousands of machines to
companies all over the world. The MG2 Group is a market leader in the
manufacture of automatic machines used to dose pharmaceuticals into hard
gelatine capsules ranging from size 000 to 5 including tamper-proof capsules. Copyright
Contify.com
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|
|
31-Dec-2009 |
31-Dec-2008 |
31-Dec-2007 |
|
Period Length |
12 Months |
12 Months |
12 Months |
|
Filed Currency |
EUR |
EUR |
EUR |
|
Exchange Rate
(Period Average) |
0.719047 |
0.683679 |
0.730637 |
|
Consolidated |
No |
No |
No |
|
|
|
|
|
|
Total income |
29.3 |
34.0 |
31.8 |
|
Net sales |
27.9 |
31.8 |
31.7 |
|
Other operating income |
0.8 |
0.6 |
0.9 |
|
Raw materials and consumables employed |
3.3 |
4.3 |
4.1 |
|
Other expenses |
12.7 |
14.7 |
11.9 |
|
Total payroll costs |
11.7 |
12.9 |
11.6 |
|
Fixed asset depreciation and amortisation |
0.5 |
0.6 |
0.6 |
|
Other operating costs |
0.4 |
0.7 |
1.5 |
|
Net operating income |
0.7 |
1.0 |
2.1 |
|
Total financial income |
0.0 |
0.1 |
- |
|
Total expenses |
0.4 |
0.4 |
0.4 |
|
Profit before tax |
0.4 |
0.6 |
1.3 |
|
Extraordinary result |
0.0 |
- |
- |
|
Profit after extraordinary items and before tax |
0.4 |
0.6 |
1.3 |
|
Total taxation |
0.4 |
0.5 |
0.7 |
|
Net profit |
- |
0.2 |
0.6 |
|
Net loss |
0.1 |
- |
- |
|
|
|
Annual Balance
Sheet |
|
Financials in:
USD (mil) |
|
|
|
|
|
31-Dec-2009 |
31-Dec-2008 |
31-Dec-2007 |
|
Filed Currency |
EUR |
EUR |
EUR |
|
Exchange Rate |
0.696986 |
0.719399 |
0.683971 |
|
Consolidated |
No |
No |
No |
|
|
|
|
|
|
Total stockholders equity |
6.5 |
6.3 |
6.5 |
|
Provision for risks |
2.9 |
2.5 |
2.6 |
|
Provision for pensions |
3.3 |
3.6 |
4.0 |
|
Mortgages and loans |
3.6 |
1.7 |
0.7 |
|
Trade creditors |
5.7 |
4.7 |
4.4 |
|
Bank loans and overdrafts |
1.3 |
2.7 |
5.8 |
|
Other current liabilities |
7.1 |
6.3 |
10.9 |
|
Accruals and deferred income |
0.0 |
0.0 |
- |
|
Total current liabilities |
14.1 |
13.7 |
21.1 |
|
Total liabilities (including net worth) |
30.4 |
27.8 |
35.0 |
|
Intangibles |
1.9 |
0.9 |
0.9 |
|
Total tangible fixed assets |
0.8 |
0.9 |
1.0 |
|
Long-term investments |
0.0 |
0.0 |
0.0 |
|
Total financial assets |
0.0 |
0.0 |
0.0 |
|
Receivables due after 1 year |
0.0 |
0.5 |
0.5 |
|
Total non-current assets |
2.8 |
2.4 |
2.4 |
|
Finished goods |
14.5 |
14.5 |
13.7 |
|
Net stocks and work in progress |
15.2 |
15.1 |
14.2 |
|
Trade debtors |
9.7 |
8.7 |
15.0 |
|
Other receivables |
1.1 |
1.0 |
1.2 |
|
Cash and liquid assets |
1.3 |
0.4 |
1.9 |
|
Accruals |
0.3 |
0.2 |
0.2 |
|
Total current assets |
27.6 |
25.4 |
32.5 |
|
Total assets |
30.4 |
27.8 |
35.0 |
|
|
|
Annual Ratios |
|
Financials in:
USD (mil) |
|
|
|
|
|
31-Dec-2009 |
31-Dec-2008 |
31-Dec-2007 |
|
Period Length |
12 Months |
12 Months |
12 Months |
|
Filed Currency |
EUR |
EUR |
EUR |
|
Exchange Rate |
0.696986 |
0.719399 |
0.683971 |
|
Consolidated |
No |
No |
No |
|
|
|
|
|
|
Sales per employee |
0.19 |
0.21 |
0.22 |
|
Profit per employee |
0.00 |
0.00 |
0.01 |
|
Average wage per employee |
0.08 |
0.09 |
0.08 |
|
Net worth |
6.5 |
6.3 |
6.5 |
|
Number of employees |
200 |
200 |
200 |
FOREIGN EXCHANGE RATES
|
Currency |
Unit
|
Indian Rupees |
|
US Dollar |
1 |
Rs.45.95 |
|
|
1 |
Rs.75.76 |
|
Euro |
1 |
Rs.66.01 |
RATING EXPLANATIONS
|
RATING |
STATUS |
PROPOSED CREDIT LINE |
|
|
>86 |
Aaa |
Possesses an extremely sound financial base with the strongest
capability for timely payment of interest and principal sums |
Unlimited |
|
71-85 |
Aa |
Possesses adequate working capital. No caution needed for credit
transaction. It has above average (strong) capability for payment of interest
and principal sums |
Large |
|
56-70 |
A |
Financial & operational base are regarded healthy. General
unfavourable factors will not cause fatal effect. Satisfactory capability for
payment of interest and principal sums |
Fairly Large |
|
41-55 |
Ba |
Overall operation is considered normal. Capable to meet normal
commitments. |
Satisfactory |
|
26-40 |
B |
Capability to overcome financial difficulties seems comparatively
below average. |
Small |
|
11-25 |
Ca |
Adverse factors are apparent. Repayment of interest and principal sums
in default or expected to be in default upon maturity |
Limited with
full security |
|
<10 |
C |
Absolute credit risk exists. Caution needed to be exercised |
Credit not
recommended |
|
-- |
NB |
New Business |
-- |
This score serves as a reference to assess SC’s credit risk
and to set the amount of credit to be extended. It is calculated from a
composite of weighted scores obtained from each of the major sections of this report.
The assessed factors and their relative weights (as indicated through %) are as
follows:
Financial
condition (40%) Ownership
background (20%) Payment
record (10%)
Credit history
(10%) Market trend
(10%) Operational
size (10%)
This report is issued at your request without any risk
and responsibility on the part of MIRA INFORM PRIVATE LIMITED (MIPL) or its
officials.