Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment.
The amino acid sequence of peptide CB-II, the major product (mol.wt. 30 000) of CNBr cleavage of fragment Bb from human complement Factor B, is given. The sequence was obtained from peptides derived by trypsin cleavage of peptide CB-II and clostripain digestion of fragment Bb. Cleavage of two Asn-Gly bonds in peptide CB-II was also found useful. These results, along with those presented in the preceding paper [Gagnon & Christie (1983) Biochem. J. 209, 51-60], yield the complete sequence of the 505 amino acid residues of fragment Bb. The C-terminal half of the molecule shows strong homology of sequence with serine proteinases. Factor B has a catalytic chain (fragment Bb) with a molecular weight twice that of proteinases previously described, suggesting that it is a novel type of serine proteinase, probably with a different activation mechanism.
D000595:Amino Acid Sequence; D002268:Carboxypeptidases; D002850:Chromatography, Gel; D011415:Complement Factor B; D003488:Cyanogen Bromide; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D004792:Enzyme Precursors; D006801:Humans; D019811:Hydroxylamine; D006898:Hydroxylamines; D010446:Peptide Fragments / Q000032:analysis*
D004792:Enzyme Precursors; D006898:Hydroxylamines; D010446:Peptide Fragments; D019811:Hydroxylamine; D002268:Carboxypeptidases; D010450:Endopeptidases; C022633:serine carboxypeptidase; D011415:Complement Factor B; D003546:Cysteine Endopeptidases; C019913:clostripain; D003488:Cyanogen Bromide