Open AccessPrimary Structure of the B‐Chain of Human Plasmin
Author(s) -
WIMAN Björn
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11578.x
Subject(s) - cyanogen bromide , plasmin , chymotrypsin , chemistry , protein primary structure , serine , proteases , biochemistry , stereochemistry , sequence (biology) , chain (unit) , peptide sequence , trypsin , enzyme , gene , physics , astronomy
The primary structure of the human plasmin B‐chain has been determined. It consists of 230 residues divided in three cyanogen bromide fragments: The amino‐terminal 24 residues, the carboxy‐terminal three residues and the middle 203 residues. Sequence determination was performed on the tryptic and the chymotryptic peptides obtained from the main cyanogen bromide fragment of this chain. Owing to similarities between some of the overlapping chymotryptic peptides, two different sequences were possible from these results. However, since the homologies with the pancreatic serine proteases and also the B‐chains of thrombin and factor XA are pronounced, the arrangement still could be settled. By peptic digestion of partially reduced and S‐carboxymethylated B‐chain it was shown that there are two interchain disulphide bridges, which connect the A and B‐chains of plasmin, involving Cys‐5 and Cys‐105 from the B‐chain. The intrachain disulphides in the B‐chain seem to be situated exactly as in chymotrypsin as partly judged from homologies.