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Binding properties of the stilbene disulfonate sites on human erythrocyte AE1: kinetic, thermodynamic, and solid state deuterium NMR analyses.

Abstract:

A novel stilbene disulfonate, 4-trimethylammonium-4'-isothiocyanostilbene-2,2'-disulfonic acid (TIDS), has been chemically synthesized, and the interaction of this probe with human erythrocyte anion exchanger (AE1) was characterized. Covalent labeling of intact erythrocytes by [N(+)((14)CH(3))(3)]TIDS revealed that specific modification of AE1 was achieved only after removal of other ligand binding sites by external trypsinization. Following proteolysis, (1.2 +/- 0.4) x 10(6) TIDS binding sit...

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Publication status:
Published

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Publisher copy:
10.1021/bi990618p

Authors


Taylor, AM More by this author
Gröbner, G More by this author
Williamson, PT More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Biochemistry
Volume:
38
Issue:
34
Pages:
11172-11179
Publication date:
1999-08-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:58dc14d5-b275-487b-8a49-b04018b45bc0
Source identifiers:
410478
Local pid:
pubs:410478

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