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PMID: 41891 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Acidic thiol proteinase activity of Schistosoma mansoni egg extracts.

The Journal of parasitology ·Vol. 65 ·No. 4 ·1979-08-00 ·Pages 543-9

Asch HL, Dresden MH

Abstract

Extracts of the eggs of the human blood fluke, Schistosoma mansoni, exhibit proteolytic activity which requires the presence of added thiol reagents or cyanide. The pH optimum for hydrolysis of Azocoll and cartilage proteoglycan is 4.8--5.2 and the molecular weight of the major component is 25--26,000. The effects of inhibitors suggest this activity belongs to the acidic thiol proteinase class, with a similarity to Cathepsin B. These proteinases may be involved in nutrition of the egg or sporocyst, in penetration of eggs or miracidia through host tissues, or in the immunopathology of schistosomiasis.

MeSH Terms
Animals Cyanides/pharmacology Endopeptidases/metabolism Female Hydrogen-Ion Concentration Intestines/parasitology Liver/parasitology Mice Molecular Weight Ovum/enzymology Protease Inhibitors Schistosoma mansoni/enzymology Schistosomiasis/parasitology Substrate Specificity Sulfhydryl Reagents/pharmacology Tissue Extracts
Chemicals
Cyanides Protease Inhibitors Sulfhydryl Reagents Tissue Extracts Endopeptidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Asch H L
Dresden M H
Article Info
Journal
The Journal of parasitology
Abbr.
J Parasitol
ISSN
0022-3395
Published
1979-08-00
Pages
543-9
Language
English
Region
United States
NLM ID
7803124
Subset
IM
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