Properties of extracellular proteinase—an activator of protein C in blood plasma formed by Aspergillus ochraceus

The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the bas...

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Published inApplied biochemistry and microbiology Vol. 51; no. 1; pp. 95 - 101
Main Authors Osmolovskiy, A. A, Kreyer, V. G, Baranova, N. A, Kurakov, A. V, Egorov, N. S
Format Journal Article
LanguageEnglish
Published Moscow Springer-Verlag 2015
Pleiades Publishing
Springer Nature B.V
Subjects
Agkistrodon contortrix
Agkistrodon contortrix contortrix
Aspergillus alutaceus
Aspergillus ochraceus
Biochemistry
Biomedical and Life Sciences
Blood
blood plasma
blood proteins
Cellular biology
Glycosylation
Life Sciences
Medical Microbiology
Microbiology
Micromycetes
molecular weight
Plasma
plasmin
Proteins
serine
substrate specificity
Substrates
venoms
Chromopeptide
Chromogenic Peptide Substrate
Thrombin Substrate
Apply Biochemistry
Aspergillus Ochraceus
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Summary:The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of Aspergillus ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase-protein C activator, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0–9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agk. contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA.
Bibliography:http://dx.doi.org/10.1134/S0003683815010123
ObjectType-Article-1
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content type line 23
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683815010123