Bile salt activation of human cholesterol esterase does not require protein dimerisation

FEBS Letters

Senior, Hugh E.J.²  Loomes, Kerry M.¹ 

[1] Biochemistry and Molecular Biology Group, School of Biological Sciences, University of Auckland, Auckland, New Zealand;Department of Health Science, UNITEC Institute of Technology, Auckland, New Zealand

关键词: Cholesterol esterase;    Lysophospholipase;    Carboxylester lipase;    Bile salt activation;    Bile salt-stimulated lipase;   

DOI  :  10.1016/S0014-5793(97)00215-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human milk cholesterol esterase (bile salt-activated lipase) plays a role in the dietary uptake of triacylglyceride and cholesteryl ester. The activities toward these substrates are mediated through a unique bile salt-activated mechanism. Previously, it has been proposed that a necessary step in this process is prior protein dimerisation in the presence of primary bile salts. In this study, we addressed the role of protein dimerisation by investigating bile salt interactions on full length and truncated recombinant forms, as analysed by size exclusion chromatography and concanavalin A Sepharose binding experiments. The present findings demonstrate that protein dimerisation is not an obligatory component of the bile salt-activated pathway. A new functional role for the glycosylated C-terminal domain in cholesterol esterase is also demonstrated in the prevention of non-specific hydrophobic interactions.

【 授权许可】

Unknown