Limited proteolysis of porcine pancreatic lipase. Lability of the Phe 335-Ala 336 bond towards chymotrypsin.
Mild chymotrypsin digestion of native lipase (449 amino acids) preferentially cleaved the Phe 335-Ala 336 bond. On SDS-gel electrophoresis, 3 major bands were observed: band 1 (52 kDa) representing native lipase, bands 2 and 3 (40 and 12 kDa) representing the two lipase fragments A and B. Fragment A does not retain lipase activity but maintains its ability to adsorb to interfaces. Fragment B was identified with the lipase C-terminal region (336-449). It does not exhibit any activity towards tributyrylglycerol emulsions and any ability to adsorb to interfaces.
D000409:Alanine; D000818:Animals; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008049:Lipase / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D010446:Peptide Fragments / Q000378:metabolism; D010649:Phenylalanine; D013379:Substrate Specificity; D013552:Swine
D010446:Peptide Fragments; D010649:Phenylalanine; D008049:Lipase; D002918:Chymotrypsin; D000409:Alanine