Literature DB >> 6715351

Anthraniloyl-tyrosine 411 as a spectroscopic probe of fatty acid binding to human serum albumin.

N Hagag, R A McPherson, E R Birnbaum, D W Darnall.   

Abstract

Reaction of human serum albumin with p-nitrophenylanthranilate results in transesterification of the anthraniloyl group to tyrosine 411. Titration of anthraniloyl-Tyr-411-albumin with long chain or short chain fatty acids produces marked changes in the absorption and fluorescence spectra of the anthraniloyl moiety as fatty acids bind in the channel near it. It appears that the anthraniloyl group is a very sensitive probe that can follow binding of small molecules at the 3-AB subdomain of human serum albumin.

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Year:  1984        PMID: 6715351

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin.

Authors:  J A Hamilton; S Era; S P Bhamidipati; R G Reed
Journal:  Proc Natl Acad Sci U S A       Date:  1991-03-15       Impact factor: 11.205

2.  Spontaneous transfer of monoacyl amphiphiles between lipid and protein surfaces.

Authors:  J B Massey; D H Bick; H J Pownall
Journal:  Biophys J       Date:  1997-04       Impact factor: 4.033

3.  Stopped-flow kinetic analysis of long-chain fatty acid dissociation from bovine serum albumin.

Authors:  Erland J F Demant; Gary V Richieri; Alan M Kleinfeld
Journal:  Biochem J       Date:  2002-05-01       Impact factor: 3.857

  3 in total

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