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Purification of human erythrocyte phosphoglycerate kinase by dye ligand affinity chromatography

✍ Scribed by Josiane Chen-Marotel; Yves Blouquit; Raymonde Rosa; Marie-Claude Calvin

Publisher: Elsevier Science
Year: 1983
Tongue: English
Weight: 906 KB
Volume: 258
Category: Article
ISSN: 1873-3778
DOI: 10.1016/s0021-9673(00)96414-8

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✦ Synopsis

A new method for the purification of human erythrocyte phosphoglyceratekinase involving affinity chromatography on dye-ligand media (Red A), in the presence of 3-phosphoglycerate and ATP, is described. The method is rapid and technically simple. The purity of the enzyme was verified by electrophoresis in polyacrylamide gel in the presence of sodium dodecylsulphate, by amino acid analysis and by immunoprecipitation in Ouchterlony plates. Peptide mapping of tryptic digests of the purified enzyme was performed and the immunoneutralization of the enzyme activity evaluated with rabbit antibodies.

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