title: Scission of human apolipoprotein B-100 by kallikrein: characterization of the cleavage site.
abstract: Low density lipoprotein (LDL) from human plasma was digested with the specific endoprotease, kallikrein. Apolipoprotein B-100, the protein moiety of LDL, was cleaved by kallikrein into two fragments (K1 and K2) which we have compared to the naturally occurring fragments, B-74 and B-26. We have found that K1 and K2 precisely match B-74 and B-26 with respect to molecular weight, stoichiometry, and amino terminal amino acid sequence. These findings provide strong evidence that kallikrein is the agent responsible for the formation of B-74 and B-26 in human LDL.
mesh_terms: D000595:Amino Acid Sequence; D053299:Apolipoprotein B-100; D001055:Apolipoproteins B / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D007610:Kallikreins / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D053299:Apolipoprotein B-100; D001055:Apolipoproteins B; D010446:Peptide Fragments; D007610:Kallikreins