Open AccessPrimary Structure of the Bovine β‐Crystallin Bp Chain
Author(s) -
DRIESSEN Huub P. C.,
HERBRINK Paul,
BLOEMENDAL Hans,
JONG Wilfricd W.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06433.x
Subject(s) - cyanogen bromide , edman degradation , crystallin , homology (biology) , protein primary structure , peptide sequence , gene duplication , chemistry , biochemistry , biology , amino acid , gene
The major polypeptide chain of bovine β‐crystallin, βBp, was fragmented by means of cyanogen bromide treatment and by enzymatic digestions. Manual and automated Edman degradation of the resulting peptides provided the complete amino acid sequence of the 0Bp chain. The N‐terminal alanine residue was shown to be N‐α‐acetylated by mass spectrometry. The chain has a length of 204 residues and a calculated molecular weight of 23210. There is a considerable degree of homology between the N‐terminal and C‐terminal halves of the chain, presumably reflecting a tandem duplication of a shorter ancestral gene. The sequence of βBp is sufficiently related to that of γ‐crystallin II to place these proteins in the same superfamily. No sequence relationship was found with the α‐crystallin chains.