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Identification of the peptide bond cleaved during activation of human Clr
Author(s) -
Arlaud Gerard J.,
Gag Jean
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81077-2
Subject(s) - chemistry , cleavage (geology) , size exclusion chromatography , peptide , protease , chromatography , gel permeation chromatography , peptide bond , peptide sequence , biochemistry , bond cleavage , enzyme , biology , organic chemistry , catalysis , paleontology , fracture (geology) , gene , polymer
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⋯