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

The intrinsic fluorescence of spectrin is strongly quenched by low concentrations of 2-bromostearate. This results from binding at a series of hydrophobic sites. Analysis of dynamic fluorescence quenching by acrylamide, iodide and caesium ions, separately and in conjunction with 2-bromostearate, lea...

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Detaylı Bibliyografya
Asıl Yazarlar: Kahana, E, Pinder, J C, Smith, K S, Gratzer, W B
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1992
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1130891/
https://ncbi.nlm.nih.gov/pubmed/1540147
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