| 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. |
