Limited proteolysis of porcine pancreatic lipase. Lability of the Phe 335-Ala 336 bond towards chymotrypsin |
| |
Authors: | M Bousset-Risso J Bonicel M Rovery |
| |
Affiliation: | Centre de Biochimie et de Biologie Moléculaire du CNRS, 31, Chemin Joseph-Aiguier, BP 71, 13402 Marseille Cedex 9, France |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|