Identification and purification of a 36 kDa bile acid binder in human hepatic cytosol.

Abstract:

:We recently purified two closely related 33 kDa proteins from rat hepatic cytosol, designated bile acid binder I and II, which selectively bind bile acids with comparable affinity as glutathione S-transferase B. This work has now been extended to human liver in which we have identified a similar cytosolic binding activity in the 30-40 kDa fraction from gel filtration. Subsequent chromatofocusing and hydroxyapatite chromatography resulted in the isolation of a homogeneous monomeric protein of 36 kDa. The binding affinity of this protein for lithocholate using the displacement of 1-anilino-8-naphthalenesulfonate (ANS) was 0.1 microM, whereas human hepatic glutathione S-transferases purified from glutathione affinity chromatography demonstrated no competitive displacement of ANS.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Stolz A,Sugiyama Y,Kuhlenkamp J,Kaplowitz N

doi

10.1016/0014-5793(84)80975-8

subject

Has Abstract

pub_date

1984-11-05 00:00:00

pages

31-5

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)80975-8

journal_volume

177

pub_type

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