Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
1.
Mikrobiologiia ; 58(6): 915-9, 1989.
Article in Russian | MEDLINE | ID: mdl-2700086

ABSTRACT

The work is concerned with studying the effect exerted by different sources of nitrogen nutrition on the biosynthesis of proteinases with a thrombolytic activity by a variant of Bacillus mesentericus, strain 64, obtained with the aid of analytical selection. Protein substrates taken as a nitrogen source stimulate the synthesis of proteinases by the bacterial culture. These enzymes have a high caseinolytic and thrombolytic activity, and the level of their activity correlates with the amount of a protein substrate added to the medium. Ammonium acetate and succinate are the best stimulants for the formation of proteinases when the salts of mineral and organic acids are used as a source of nitrogen nutrition. In that case, the enzymes have a high thrombolytic activity and a low caseinolytic activity. A semi-synthetic medium with the aforementioned nitrogen-containing compounds as a source of nitrogen nutrition is proposed for the synthesis of thrombolytic proteinase by the variant of B. mesentericus.


Subject(s)
Bacillus/enzymology , Endopeptidases/biosynthesis , Fibrinolysis , Nitrogen/metabolism , Bacillus/growth & development , Clot Retraction , Culture Media , Endopeptidases/metabolism , Humans
2.
Mikrobiologiia ; 57(3): 394-7, 1988.
Article in Russian | MEDLINE | ID: mdl-3054437

ABSTRACT

The effect of some inhibitors and bivalent metal cations (Mn2+, Ca2+, Fe2+, Zn2+, Mg2+, Co2+ and Cu2+) on the proteolytic activity of two Bacillus mesentericus strains (strain 8 and strain 64 M-variant) was comparatively studied. The both enzymes were shown to be serine proteinases, but the proteinase of strain 64 was also a metal-dependent enzyme. Metal ions exerted no essential effect on the proteinase of strain 8. Ca2+ and Mg2+ ions stimulated the proteinase activity of strain 64 whereas Fe2+ and Zn2+ ions inhibited it in the case of three substrates. Therefore, the two proteinases are different.


Subject(s)
Bacillus/drug effects , Metals/pharmacology , Protease Inhibitors/pharmacology , Aspergillus/drug effects , Aspergillus/enzymology , Bacillus/enzymology , Cations , Fibrinolysis/drug effects , Humans , Peptide Hydrolases/pharmacology
3.
Mikrobiologiia ; 56(6): 947-50, 1987.
Article in Russian | MEDLINE | ID: mdl-3329699

ABSTRACT

The natural variability of the ability to synthesize proteinases by Bacillus mesentericus 64 was studied. The population of this strain was shown to be heterogeneous. Three types of variants (S, M and P) differed in the morphology of their colonies and in the culture characteristics from the typical colonies of the parent strain. The caseinolytic activity of the M variant was three times as high as that of the parent strain, and it also had an elevated fibrinolytic activity and a high rate of blood thrombolysis in experiments in vitro. The rate of proteinase synthesis correlated with the morphological types of sporogenic bacteria.


Subject(s)
Bacillus/enzymology , Fibrinolysis/drug effects , Genetic Variation , Peptide Hydrolases/pharmacology , Caseins/metabolism , Culture Media/metabolism , Fibrin/metabolism , Peptide Hydrolases/biosynthesis
SELECTION OF CITATIONS
SEARCH DETAIL
...