Open AccessThe Amino‐Acid Sequence of the αA 2 Chain of Bovine α‐Crystallin
Author(s) -
Ouderaa Frans J.,
Jong Wilfried W.,
Bloemendal Hans
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03119.x
Subject(s) - cyanogen bromide , edman degradation , chemistry , digestion (alchemy) , sequence (biology) , peptide sequence , chain (unit) , chromatography , trypsin , cyanogen , protein primary structure , biochemistry , organic chemistry , enzyme , gene , physics , astronomy
The αA 2 chain of bovine α‐crystallin was fragmented by means of cyanogen bromide treatment and by tryptic, chymotryptic and thermolytic digestions. Twenty tryptic peptides were obtained from the S‐aminoethylated αA 2 chain, accounting together for the complete sequence. The direct Edman degradation and the dansyl‐Edman technique were used to determine the sequences of the tryptic peptides. The order of the tryptic peptides was deduced from overlapping peptides obtained by cyanogen bromide treatment, tryptic digestion of the maleylated chain and chymotryptic and thermolytic digestion of the S‐aminoethylated chain. The sequence of the αA 2 chain comprises 173 residues and corresponds to a molecular weight of 19 832.