Some properties of the protease from Aspergillus terricola

The protease from Aspergillus terricola (terrilytin) was isolated and purified by the ion exchange method and by gel chromatography. The data on its molecular weight, isoelectric point, N-terminal amino acids were described. The protease included polysaccharide which stabilized the enzyme activity u...

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Bibliographic Details
Published in:Mycopathologia (1975) 1975-11, Vol.56 (3), p.153-157
Main Authors: Zaikina, N A, Shataeva, L K, Elinov, N P, Samsonov, G V
Format: Article
Language:English
Subjects:
Animals
Aspergillus - enzymology
Chemical Phenomena
Chemistry
Fibrinolysis - drug effects
Fibrinolytic Agents - pharmacology
Hydrolysis
Oligopeptides
Peptide Hydrolases - immunology
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
Polysaccharides - metabolism
Polysaccharides - pharmacology
Proteins
Rabbits
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Summary:The protease from Aspergillus terricola (terrilytin) was isolated and purified by the ion exchange method and by gel chromatography. The data on its molecular weight, isoelectric point, N-terminal amino acids were described. The protease included polysaccharide which stabilized the enzyme activity under the storage and lyophylization. Polysaccharides isolated from different fungi and yeasts were found to stabilize and activate terrilytin rising the affinity of enzyme to substrate. Terrilytin was revealed to exhibit the thrombolytic effect and expressive affinity to the fibrin in comparison with other substrates of high and low molecular weight. The enzyme showed the antigenic activity. From immune rabbit sera 7S gamma-globulins inhibiting proteolysis of caseine and 19S gamma-globulins activating the proteolysis of fibrin and fibrinogen by terrilytin were isolated by gel chromatography.
ISSN:0301-486X
1573-0832
DOI:10.1007/BF02093314