Limited proteolysis of porcine pancreatic lipase

FEBS Letters

Bonicel, J.¹  Rovery, M.¹  Bousset-Risso, M.¹ 

[1] Centre de Biochimie et de Biologie Moléculaire du CNRS, 31, Chemin Joseph-Aiguier, BP 71, 13402 Marseille Cedex 9, France

关键词: Limited proteolysis;    Protease susceptibility;    Chymotrypsin digestion;    Domain structure;    Interface adsorption;    Triacylglycerol lipase;    (Porcine pancreas);   

DOI  :  10.1016/0014-5793(85)80325-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown