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Purification and characterization of a 47 kDa protease from Schistosoma mansoni cercarial secretion

Published online by Cambridge University Press:  06 April 2009

C. Chavez-Olortegui
Affiliation:
Departamento de Bioquímica-Imunologia e, Instituto de Ciêencias Biológicas da Universidade Federal de Minas Gerais, CP 2486–30161 Belo Horizonte, MG, Brazil
M. Resende
Affiliation:
Microbiologia, Instituto de Ciências Biológicas da Universidade Federal de Minas Gerais, CP 2486–30161 Belo Horizonte, MG, Brazil
C. A. P. Tavares
Affiliation:
Departamento de Bioquímica-Imunologia e, Instituto de Ciêencias Biológicas da Universidade Federal de Minas Gerais, CP 2486–30161 Belo Horizonte, MG, Brazil

Summary

Fractionation of Schistosoma mansoni cercariae gland secretion on a Sephadex G-150 column followed by a Superose-12 column in an FPLC system, isolated a 47 kDa protease which migrated as a single band on SDS–PAGE gels. A monoclonal antibody (MAb) was produced which recognizes only the 47 kDa protease, and an immuno-affinity column with the MAb was used to isolate the protease. The 47 kDa protease showed activity on several macromolecules such as elastin and collagen type VI besides gelatin and casein. This suggests that this enzyme can be one of the enzymes that might facilitate invasion of the cercariae through host skin. The optimal pH of the protease against the synthetic substrate, Ac-Phe-Arg-Nan, in Tris–HCI buffer was 10. Experiments with protease inhibitors indicate that the purified enzyme is a serine protease.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1992

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References

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