Amino acid sequence studies of human C4b-binding protein: N-terminal sequence analysis and alignment of the fragments produced by limited proteolysis with chymotrypsin and the peptides produced by cyanogen bromide treatment.
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Chung LP, Gagnon J, Reid KB
Amino acid sequence studies of human C4b-binding protein: N-terminal sequence analysis and alignment of the fragments produced by limited proteolysis with chymotrypsin and the peptides produced by cyanogen bromide treatment.
Mol Immunol. 1985 Apr;22(4):427-35.
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- 4033666 [ View in PubMed]
- Abstract
Treatment of human C4b-binding protein (C4BP) with cyanogen bromide gave five major peptides and limited proteolysis with chymotrypsin yielded two fragments. The yields, apparent mol. wts and N-terminal amino acid sequences of these peptides and fragments indicates that in dissociating conditions, after reduction of disulphide bonds, C4BP is composed of only one type of polypeptide chain of approx. 70,000 mol. wt. The amino acid sequence data obtained, which accounts for over 55% of the total sequence, allows an alignment of the cyanogen bromide peptides. In addition the amino acid sequence data indicates that the 70,000-dalton polypeptide chain of C4BP contains nine internal homology regions, each 60 amino acids long, which would account for 540 of the expected 600 amino acids in C4BP. Similar internal homology regions are found within the Ba region of factor B [Morley and Campbell, EMBO J. 3, 153-157 (1984)] and it is of interest that the regions found in C4BP are homologous to those found in Ba.