NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange

NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange

Two lines of evidence are presented to indicate that that the N-(4-azido-2-nitrophenyl)-2-aminoethyl sulfonate (NAP-taurine) and N-(4-isothiocyano-2-nitrophenyl)-2-aminoethyl sulfonate sites are identical or located very close to each other. The cross-linking agent has parallel effects on the noncom...

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Veröffentlicht in:American Journal of Physiology: Cell Physiology 1995-08, Vol.38 (2), p.c410-c416
Hauptverfasser: KNAUF, P. A, SPINELLI, L. J
Format: Artikel
Sprache:eng
Schlagworte:
Analytical, structural and metabolic biochemistry
Binding and carrier proteins
Biochemistry
Biological and medical sciences
Cellular biology
Erythrocytes
Fundamental and applied biological sciences. Psychology
Proteins
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Beschreibung
Zusammenfassung:Two lines of evidence are presented to indicate that that the N-(4-azido-2-nitrophenyl)-2-aminoethyl sulfonate (NAP-taurine) and N-(4-isothiocyano-2-nitrophenyl)-2-aminoethyl sulfonate sites are identical or located very close to each other. The cross-linking agent has parallel effects on the noncompetitive inhibition exerted by either external iodide or NAP-taurine.
ISSN:0363-6143
1522-1563