Abstract
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.
MeSH Terms
Amino Acid Sequence
Carboxypeptidases
Chromatography, Gel
Complement Factor B
Cyanogen Bromide
Cysteine Endopeptidases
Endopeptidases
Enzyme Precursors
Humans
Hydroxylamine
Hydroxylamines
Peptide Fragments/analysis
Chemicals
Enzyme Precursors
Hydroxylamines
Peptide Fragments
Hydroxylamine
Carboxypeptidases
Endopeptidases
serine carboxypeptidase
Complement Factor B
Cysteine Endopeptidases
clostripain
Cyanogen Bromide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Christie D L
Gagnon J
References (18)
18 references, click to expand
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