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Proteolytic cleavage of IgG bound to the Fc receptor of Schistosoma mansoni schistosomula

 

作者: C. AURIAULT,   M.A. OUAISSI,   G. TORPIER,   H. EISEN,   A. CAPRON,  

 

期刊: Parasite Immunology  （WILEY Available online 1981）
卷期: Volume 3, issue 1  

页码: 33-44

 

ISSN:0141-9838

 

年代: 1981

 

DOI:10.1111/j.1365-3024.1981.tb00383.x

 

出版商: Blackwell Publishing Ltd

 

关键词: Keywords:Schistosoma mansoni;IgG;Fc receptor;proteolytic enzymes

 

数据来源: WILEY

 

摘要:

SUMMARYAfter the binding of IgG to the surface Fc receptor of Schistosoma mansoni schistosomula, the Fab portions of IgG are cleaved and small peptides are liberated in the culture medium. At least two types of proteinase activities have been demonstrated in the secretory products of schistosomula. One is an endoprotease with trypsin‐like activity, with an optimum pH of 7 and an optimum temperature of 45°C. The other is a metalloaminopeptidase with an optimum pH of 7 and temperature of 37

 

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