An association between Schistosoma mansoni worms and an enzymatically-active protease/peptidase in mouse blood.
An enzyme found previously in extracts of adult Schistosoma mansoni worms, that hydrolysed the chromogenic substrate N-acetyl-DL-phenylalanine beta-naphthyl-ester, has here been further investigated and characterized. Evidence that the molecule found in the parasite was antigenically and enzymatically homologous with a constituent of normal mouse plasma has been consolidated using a monospecific serum in immunoelectrophoresis and Western immunoblotting. The molecular size of the enzyme was found to be approximately 70 kDa and it was inhibited by a serine protease inhibitor, but not by inhibitors of other classes of protease. The enzymatic activity found in normal mouse serum was also found in normal rat serum, but not in sera from several other mammalian species.
Darani
H Y
HY
School of Biological Sciences, University of Bangor, Bangor, Gwynedd LL57 2UW, UK. H_yousofi@yahoo.com
Doenhoff
M J
MJ
D000818:Animals; D003378:Counterimmunoelectrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D051379:Mice; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012550:Schistosoma mansoni / Q000201:enzymology*; D012555:Schistosomiasis mansoni / Q000201:enzymology* / Q000469:parasitology; D012697:Serine Endopeptidases / Q000097:blood* / Q000302:isolation & purification / Q000378:metabolism
D011480:Protease Inhibitors; C013791:N-acetylphenylalanine beta-naphthyl ester; D010649:Phenylalanine; D012697:Serine Endopeptidases