Crossref journal-article
Portland Press Ltd.
Biochemical Journal (288)
Abstract

The interaction of human serum albumin with monomeric haemin has been investigated by detailed kinetic analysis in dimethyl sulphoxide/water (3:5, v/v). The results obtained under conditions of albumin saturation of haemin and under pseudo-single turnover conditions indicate that methaemalbumin is formed in a two-stage, single-intermediate process. The initial association between the haemin and human serum albumin is a chemically controlled process (k1 = 1.7 × 10(5) mol-1 . s-1 . dm3 at 24 degrees C); the variation of K1 with pH exhibited a well defined pK of 5.9. The overall equilibrium constant, calculated by using microscopic rate constants, is 1.1 (+/- 0.5) X 10(8) mol-1 at 24 degrees C. The data and conclusions are consistent with a general binding mechanism for albumin in which intermediate formation is followed by an entropy-controlled internalization of the ligand.

Bibliography

Adams, P. A., & Berman, M. C. (1980). Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin. Biochemical Journal, 191(1), 95–102.

Authors 2
  1. P A Adams (first)
  2. M C Berman (additional)
References 0 Referenced 124

None

Dates
Type When
Created 10 years ago (Aug. 10, 2015, 4:24 p.m.)
Deposited 3 years, 9 months ago (Nov. 25, 2021, 7:24 a.m.)
Indexed 11 months, 2 weeks ago (Sept. 13, 2024, 12:42 p.m.)
Issued 44 years, 10 months ago (Oct. 1, 1980)
Published 44 years, 10 months ago (Oct. 1, 1980)
Published Print 44 years, 10 months ago (Oct. 1, 1980)
Funders 0

None

@article{Adams_1980, title={Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin}, volume={191}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1910095}, DOI={10.1042/bj1910095}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Adams, P A and Berman, M C}, year={1980}, month=oct, pages={95–102} }