Literature DB >> 1648396

EPR study of the hydrophobic interaction of spectrin with fatty acids.

S Streichman1, E Kahana, B L Silver.   

Abstract

The hydrophobic interaction between spin-labelled stearic acid and spectrin was studied by electron paramagnetic resonance (EPR) and fluorescence quenching. The results are quantitatively interpreted in terms of two types of binding site on spectrin. A comparison between the results of the EPR and fluorescence experiments show the drawback of the fluorescence method in binding studies.

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Year:  1991        PMID: 1648396     DOI: 10.1016/0005-2736(91)90243-2

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


  1 in total

1.  Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites.

Authors:  E Kahana; J C Pinder; K S Smith; W B Gratzer
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

  1 in total

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