Partial purification of a high affinity taurine binding protein by affinity chromatography

Taurine (2-aminoethanesulfonic acid) is a ubiquitous amino acid found in very high concentrations in mammalian tissues. Recently, high affinity taurine binding sites were identified, detergent solubilized, and shown to have affinities similar to the beta -amino acid transport system. In this communi...

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Veröffentlicht in:	Biochemical pharmacology 1983-02, Vol.32 (4), p.753-756
Hauptverfasser:	Kulakowski, Elliott C., Schaffer, Stephen W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Brain Chemistry Carrier Proteins - isolation & purification Chromatography, Affinity heart Myocardium - analysis pigs sarcolemma Sarcolemma - analysis Solubility Swine taurine
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container_title	Biochemical pharmacology
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creator	Kulakowski, Elliott C. Schaffer, Stephen W.
description	Taurine (2-aminoethanesulfonic acid) is a ubiquitous amino acid found in very high concentrations in mammalian tissues. Recently, high affinity taurine binding sites were identified, detergent solubilized, and shown to have affinities similar to the beta -amino acid transport system. In this communication, the authors present for the first time an affinity chromatographic method for the purification of a high affinity taurine transport protein from cardiac sarcolemma.
doi_str_mv	10.1016/0006-2952(83)90512-9
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subjects	Animals Brain Chemistry Carrier Proteins - isolation & purification Chromatography, Affinity heart Myocardium - analysis pigs sarcolemma Sarcolemma - analysis Solubility Swine taurine
title	Partial purification of a high affinity taurine binding protein by affinity chromatography
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