Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Loomes KM,Senior HEdoi
10.1016/s0014-5793(97)00215-9subject
Has Abstractpub_date
1997-04-01 00:00:00pages
369-72issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00215-9journal_volume
405pub_type
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