Literature DB >> 43743

Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements.

J Wilting, M M Weideman, A C Roomer, J H Perrin.   

Abstract

The molar ellipticity of the warfarin-albumin complex at 310 nm increases with pH from 6 to 9. This pH dependence runs parallel with that of the molar ellipticity of the albumin alone at 292 nm. The change in molar ellipicity with pH occurs in a smaller pH interval after addition of the physiological concentration of calcium ions. These findings give support to the assumption that the binding site for warfarin on the albumin molecule is affected by the neutral-to-base transition in the protein.

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Year:  1979        PMID: 43743     DOI: 10.1016/0005-2795(79)90075-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

Review 1.  Methods of determining plasma and tissue binding of drugs. Pharmacokinetic consequences.

Authors:  G M Pacifici; A Viani
Journal:  Clin Pharmacokinet       Date:  1992-12       Impact factor: 6.447

2.  Drug binding to alpha 1-acid glycoprotein studied by circular dichroism.

Authors:  M Otagiri; R Yamamichi; T Maruyama; T Imai; A Suenaga; Y Imamura; K Kimachi
Journal:  Pharm Res       Date:  1989-02       Impact factor: 4.200

3.  Allosteric properties of the oxyphenbutazone--human serum albumin complex.

Authors:  J H Dröge; L H Janssen; J Wilting
Journal:  Pharm Weekbl Sci       Date:  1983-10-21

4.  Interspecies differences in the effect of pH on gallopamil protein binding to albumin and alpha 1-acid glycoprotein.

Authors:  D R Rutledge; M T Chong; M V Nelson
Journal:  Eur J Clin Pharmacol       Date:  1991       Impact factor: 2.953

  4 in total

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