Identification of the peptide bond cleaved during activation of human Clr

FEBS Letters

Gagnon, Jean¹  Arlaud, Gerard J.² 

[1] MRC Immunochemistry Unit,Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England;Departement de Recherches Fondamentales (U A CNRS no. 556, Unite INSERM no. 238), Laboratoire de Biologie Moleculaire et Cellulaire, CEN-Grenoble 85X, 38041 Grenoble Cedex, France

关键词: Human Clr;    Sequence;    Serine protease activation;    Limited proteolysis;   

DOI  :  10.1016/0014-5793(85)81077-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

CNBr cleavage of unreduced proenzyme Clr yielded fragment CP2b, isolated by gel filtration and highpressure gel permeation chromatography. This fragment (~ M _τ 55000) comprised at least 4 disulphidelinked peptides, which were separated by gel filtration after reduction and alkylation. Peptide CP2bRA4, overlapping the A- and B-chain regions in proenzyme Clr was digested by V8 staphylococcal protease, and the digest separated by reversed-phase HPLC. N-terminal sequence analysis of peptide CP2bRA4SP9 established that Clr activation involves the cleavage of a single Arg-Ile bond, located in the sequence:⋯ Gln-Arg-Gln-Arg-Ile-Ile-Gly-Gly⋯

【 授权许可】

Unknown