Comparative study of the fluid‐phase proteolytic cleavage of human complement subcomponents C4 and C2 by Cs and Cr2‐Cs2

FEBS Letters

Villiers, Christian L.¹  Villiers, Marie-Bernadette¹  Thielens, Nicole M.²  Colomb, Maurice G.¹ 

[1] Equipe de Recherche Immunochimie — Système Complémentaire du DRF-G et de l'USM-G, associée au CNRS (E.R.A. no. 695) et à l'INSERM (U no. 238), Grenoble Cedex, France;Laboratoire de Biologie Moléculaire et Cellulaire, Centre d'Etudes Nucléaires de Grenoble, 85X, 38041 Grenoble Cedex, France

关键词: Complement;    Protease;    Monoclonal antibody;    C2;    C4;    C1s;    SDS—PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;    the nomenclature of the components of complement is that recommended by the World Health Organization (1968);    an over bar indicates the activated state of a component.;   

DOI  :  10.1016/0014-5793(84)80025-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The C3 convertase of the classical pathway of complement is composed of fragments C4b and C2a resulting from cleavage of C4 and C2 by activated C. The limited proteolysis of these two different substrates by the same protease, Cs, has been studied in the fluid phase using purified proteins. The turnover numbers of C2 and C4 cleavage by Cs were affected to different extents, depending on whether Cs was alone or associated with Cr or with monoclonal antibodies to Cs. The binding of C2 to C4 favours the proteolysis of C2 by Cs, as revealed by the use of I₂-treated C2.

【 授权许可】

Unknown