Characteristics of the cell surface antigen, p72, associated with a variety of human tumours and mitogen-stimulated T-lymphoblasts |
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Authors: | M R Price D G Campbell R A Robins T E Blecher R W Baldwin |
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Affiliation: | 1. Institute of Applied Molecular Biology and Genetics, 125206 Moscow, USSR;2. Institute of Medical Enzymology, 123242 Moscow, USSR |
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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. |
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