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. 1987;19(7):613-8.
doi: 10.1016/0020-711x(87)90227-8.

Protein band 3 phosphotyrosyl phosphatase. Purification and characterization

P Boivin, C Galand, O Bertrand

Protein band 3 phosphotyrosyl phosphatase. Purification and characterization

P Boivin et al. Int J Biochem. 1987.

Abstract

A phosphotyrosylprotein phosphatase has been purified from human red cell cytosol by successive DEAE cellulose, phosphocellulose and Red Procion-H3B-Sepharose chromatography. Overall purification was about 9000 with a yield of 30%. The enzyme was more than 95% pure as judged by SDS polyacrylamide gel. Its molecular weight was 17,000 and maximum activity was observed at pH 5.5. It was active towards both the phosphorylated tyrosine on the cytosolic fragment of the red cell protein band 3 and para-nitrophenyl phosphate. However the effects of ligands differ for the two substrates.

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