AN ANTIBIOTIC PRODUCED BY MICROCOCCUS EPIDERMIDIS

1950 ◽  
Vol 28e (5) ◽  
pp. 212-216 ◽  
Author(s):  
L. J. Loeb ◽  
A. Moyer ◽  
R. G. E. Murray
Keyword(s):  
Molecular Weight ◽  
Streptococcus Pyogenes ◽  
Water Purification ◽  
Active Substance ◽  
Test Organism ◽  
Chemical Data ◽  
Low Molecular Weight ◽  
Heat Stable ◽  
Wide Range ◽  
Physical And Chemical

A stable antibiotic was produced by a strain of Micrococcus epidermidis that showed a wide range of activity against Gram-positive organisms. A mucoid Streptococcus pyogenes was used as test organism. This strain could be made resistant by being grown in increasing concentrations of antibiotic but the organism reverted to its original susceptibility immediately on transfer to medium without antibiotic. There was no antiluminescent activity when tested on Photobacterium fischeri. The test organism was not lysed by the antibiotic. The active substance was dialyzable, was remarkably heat stable, and was soluble only in water or, providing water was present, in solvents that were completely miscible with water. Purification was successful only to the extent of removing a number of inactive fractions by differential solubilities. The activity was destroyed by trypsin but not by pepsin. The physical and chemical data make it probable that the substance is a polypeptide of low molecular weight.

STUDIES ON THE ISOLATION AND NATURE OF THE 'TERREGENS FACTOR'

1954 ◽  
Vol 32 (1) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Ferric Iron ◽  
Test Organism ◽  
The Other ◽  
Inorganic Salts ◽  
Low Molecular Weight ◽  
Straight Chain ◽  
Heat Stable ◽  
Growth Promoting

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.

STUDIES ON THE ISOLATION AND NATURE OF THE 'TERREGENS FACTOR'

1954 ◽  
Vol 32 (4) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Ferric Iron ◽  
Test Organism ◽  
The Other ◽  
Inorganic Salts ◽  
Low Molecular Weight ◽  
Straight Chain ◽  
Heat Stable ◽  
Growth Promoting

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.

NOM and MIB, who wins in the competition for activated carbon adsorption sites?

2004 ◽  
Vol 49 (9) ◽  
pp. 257-265 ◽  
Author(s):  
C. Hepplewhite ◽  
G. Newcombe ◽  
D.R.U. Knappe
Keyword(s):  
Molecular Weight ◽  
Activated Carbons ◽  
Background Concentration ◽  
Low Molecular Weight ◽  
Activated Carbon Adsorption ◽  
Microporous Carbons ◽  
Adsorption Sites ◽  
Carbon Adsorption ◽  
Competitive Mechanism ◽  
Wide Range

The adsorption of an odour compound common in drinking water, 2-methylisoborneol (MIB), was studied on two activated carbons in the presence of 13 well-characterised natural organic matter (NOM) solutions. It was found that, although the carbons and the NOM solutions had a wide range of characteristics, the major competitive mechanism was the same in all cases. The low molecular weight NOM compounds were the most competitive, participating in a direct competition with the MIB molecule for adsorption sites. Equivalent background concentration (EBC) calculations indicated a relatively low concentration of directly competing compounds in the NOM. Some evidence of pore restriction was also seen, with microporous carbons most affected by low molecular weight NOM, and mesoporous carbons impacted by the higher molecular weight compounds.

Low molecular weight gels: potential in remediation of crude oil spillage and recovery

RSC Advances ◽  
2016 ◽  
Vol 6 (58) ◽  
pp. 53415-53420 ◽  
Author(s):  
Ch. Siva Kesava Raju ◽  
Bhaskar Pramanik ◽  
Tanmoy Kar ◽  
Peddy V. C. Rao ◽  
Nettem V. Choudary ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Crude Oil ◽  
Potential Application ◽  
Crude Oils ◽  
Low Molecular Weight ◽  
Oil Spillage ◽  
Wide Range ◽  
First Time

A molecular gelator which has strong gelation ability for different crude oils (light to heavy crudes), and a wide range of refinery products is reported for the first time for its potential application in oil spillage/recovery.

Studies on lipopolysaccharides of Proteus

1971 ◽  
Vol 17 (11) ◽  
pp. 1385-1394 ◽  
Author(s):  
B. A. Dmitriev ◽  
N. A. Hinton ◽  
R. W. Lowe ◽  
J. K. N. Jones
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Weight Fraction ◽  
Low Molecular Weight ◽  
The Core ◽  
Wide Range ◽  
Homologous Antiserum ◽  
Main Components ◽  
Different Strains ◽  
Second Peak

The polysaccharide moieties of the lipopolysaccharides of serotyped strains of Proteus have been examined. The strains were selected to provide a wide range of serotypes. The primary acetic acid extracts of different strains of Proteus were fractionated on Sephadex G-50 and yielded three main components: a peak (I), which was composed mainly of polysaccharide; a second peak (II), the core polysaccharide, which contained heptose and phosphate; and a third component (III), which corresponded to a low molecular weight fraction and contained KDO and phosphate as well as other components. Peak I was not encountered in rough strains of Proteus. The chemical composition of the peaks obtained for S, SR, and R strains is discussed in relation to their agglutinating ability to homologous antiserum.

The Characterization of Two New Low Molecular Weight Proteins (LMPs) from Streptococcus pyogenes

1992 ◽  
Vol 277 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Dieter Gerlach ◽  
Heide Alouf ◽  
Ladislav Morávek ◽  
Manfred Pavlik ◽  
Werner Köhler
Keyword(s):  
Molecular Weight ◽  
Streptococcus Pyogenes ◽  
Low Molecular Weight ◽  
Low Molecular Weight Proteins

Dipeptide-Based Low-Molecular-Weight Efficient Organogelators and Their Application in Water Purification

2008 ◽  
Vol 14 (23) ◽  
pp. 6870-6881 ◽  
Author(s):  
Sisir Debnath ◽  
Anshupriya Shome ◽  
Sounak Dutta ◽  
Prasanta Kumar Das
Keyword(s):  
Molecular Weight ◽  
Water Purification ◽  
Low Molecular Weight

A heat stable low molecular weight inhibitor of lysosomal cysteine proteinases in human serum

1983 ◽  
Vol 110 (2) ◽  
pp. 449-455 ◽  
Author(s):  
Francis Gauthier ◽  
Maurice Pagano ◽  
Frédéric Esnard ◽  
Henri Mouray ◽  
Robert Engler
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
Low Molecular Weight ◽  
Cysteine Proteinases ◽  
Heat Stable
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