Literature DB >> 9914651

Reversible binding of ethacrynic acid to human serum albumin: difference circular dichroism study.

C Bertucci1, B Nanni, P Salvadori.   

Abstract

The reversible binding of ethacrynic acid was characterized by a difference circular dichroism method. A 2/1 stoichiometry was determined for the [drug]/[HSA] (human serum albumin) complex. The reversible binding of ethacrynic acid to HSA determines direct competition with ligands that selectivity bind to site II and to the fatty acid site. Furthermore, indirect competition was shown for ligands for site I (anti-cooperative) and to site III (cooperative).

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Year:  1999        PMID: 9914651     DOI: 10.1002/(SICI)1520-636X(1999)11:1<33::AID-CHIR6>3.0.CO;2-U

Source DB:  PubMed          Journal:  Chirality        ISSN: 0899-0042            Impact factor:   2.437


  3 in total

Review 1.  Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.

Authors:  K Oettl; R E Stauber
Journal:  Br J Pharmacol       Date:  2007-04-30       Impact factor: 8.739

2.  Development of enhanced capacity affinity microcolumns by using a hybrid of protein cross-linking/modification and immobilization.

Authors:  Xiwei Zheng; Maria Podariu; Cong Bi; David S Hage
Journal:  J Chromatogr A       Date:  2015-05-01       Impact factor: 4.759

3.  Induction of axial chirality in divanillin by interaction with bovine serum albumin.

Authors:  Diego Venturini; Aguinaldo Robinson de Souza; Ignez Caracelli; Nelson Henrique Morgon; Luiz Carlos da Silva-Filho; Valdecir Farias Ximenes
Journal:  PLoS One       Date:  2017-06-02       Impact factor: 3.240

  3 in total

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