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Identification and purification of a 36 kDa bile acid binder in human hepatic cytosol
Author(s) -
Stolz Andrew,
Sugiyama Yuichi,
Kuhlenkamp John,
Kaplowitz Neil
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80975-8
Subject(s) - chromatofocusing , cytosol , affinity chromatography , glutathione , biochemistry , size exclusion chromatography , chemistry , chromatography , enzyme
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 homogenous 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 μM, whereas human hepatic glutathione S ‐transferases purified from glutathione affinity chromatography demonstrated no competitive displacement of ANS.