Interactions of rat α-foetoprotein with bilirubin

Author:

Versée V,Barel A O

Abstract

The binding of bilirubin to rat-alpha-foetoprotein has been measured by changes in the absorption spectrum and by the appearance of two intense circular-dichroism bands. Furthermore binding of this bile pigment has been demonstrated by a decrease of its enzymic oxidation rate and by competition experiments with bovine serum albumin-agarose. The binding parameters have been determined as follows: n = 1.0 mol bound/mol of protein and Ka = 2.9 × 10(6) M-1. Competition of oestradiol for the bilirubin-binding site has not been established.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Affinity of Human Serum Albumin for Bilirubin Varies with Albumin Concentration and Buffer Composition;Journal of Biological Chemistry;2001-08

2. Mechanisms for the transport of unconjugated bilirubin in human trophoblastic BeWo cells;FEBS Letters;2001-04-19

3. Chemistry and Biology of α-Fetoprotein;Advances in Cancer Research;1991

4. Heme in the treatment of heme deficiency states;Scandinavian Journal of Clinical and Laboratory Investigation;1990

5. Heme in the treatment of heme deficiency states;Scandinavian Journal of Clinical and Laboratory Investigation;1990-01

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