Inulin-induced activation of factor B in whole serum: description of structural modifications in the Ba fragment.
The investigation of inulin-induced conversion of human factor B in serum by isoelectrofocusing revealed physiological modifications in the primary structure of the Ba fragment. Evidence has been obtained that a nascent Ba, generated by the hydrolytic action of the D component on B in serum, was a short-lived product and that a fast release of carboxy-terminal arginine and lysine residues occurred involving a serum carboxypeptidase B enzyme.
D015097:3-Mercaptopropionic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D000614:Aminocaproates / Q000494:pharmacology; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000494:pharmacology; D011415:Complement Factor B / Q000378:metabolism*; D004792:Enzyme Precursors / Q000378:metabolism*; D006801:Humans; D007444:Inulin / Q000494:pharmacology*; D007525:Isoelectric Focusing
D000614:Aminocaproates; D004792:Enzyme Precursors; C029729:2-mercaptomethyl-3-guanidinoethylthiopropionic acid; D007444:Inulin; D015097:3-Mercaptopropionic Acid; D002268:Carboxypeptidases; D043424:Carboxypeptidase B; D011415:Complement Factor B