Open AccessAmino acid sequence of the beta chain of human fibrinogen: homology with the gamma chain.
Author(s) -
K W Watt,
Takashi Takagi,
Russell F. Doolittle
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.4.1731
Subject(s) - cyanogen bromide , fibrinogen , peptide sequence , homology (biology) , alpha chain , chemistry , amino acid , biochemistry , chain (unit) , beta (programming language) , stereochemistry , gene , physics , astronomy , computer science , programming language
The beta chain of human fibrinogen is composed of 452 +/- 5 amino acid residues, 14 of which are methionines. Consistent with these findings we have isolated and characterized 15 fragments after cyanogen bromide digestion of carboxymethylated beta chains. The arrangement of several of these peptides was deduced on the basis of overlapping peptides isolated from the fragments D and E produced by the plasmic digestion of fibrinogen and/or from a tryptic digest of citraconylated beta chains. Most of the other cyanogen bromide fragments can be aligned by homology with the alpha and/or gamma chains from human fibrinogen, although the positioning of a few of the smallest peptides is still ambiguous. The homology of the beta chain with the gamma chain is especially strong in certain regions of the domain that includes fragment D.