Proteolytic digestion of human serum apolipoproteins by porcine pancreatic elastase.
We studied the proteolytic action in vitro of free and alpha 2-macroglobulin-bound porcine pancreatic elastase [EC 3.4.21.11] on the apolipoproteins of plasma: very low density lipoprotein (VLDL), low density lipoprotein (LDL), and high density lipoprotein (HDL). Polyacrylamide gel electrophoresis, isoelectric focusing and immunodiffusion tests of elastase-treated plasma lipoproteins revealed that apolipoprotein C-II and C-III polypeptides were more susceptible to elastase in free form than plasma apolipoproteins (A-I, A-II, B, and E). Elastase bound to alpha 2-macroglobulin did not show any such activities.
D000818:Animals; D001053:Apolipoproteins / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D013552:Swine; D000511:alpha-Macroglobulins / Q000378:metabolism
D001053:Apolipoproteins; D000511:alpha-Macroglobulins; D010196:Pancreatic Elastase