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J. Biol. Chem., Vol. 263, Issue 14, 6722-6730, May, 1988
NK Tonks, CD Diltz and EH Fischer
This report describes the purification of the major protein-tyrosine-
phosphatases from human placenta. Enzyme activity was followed with a novel
artificial substrate, namely reduced, carboxamidomethylated, and maleylated
lysozyme, phosphorylated on tyrosine by a partially purified preparation of
insulin and epidermal growth factor receptor kinases, also from human
placenta. The key step in the purification of the
protein-tyrosine-phosphatases was affinity chromatography on a column of
thiophosphorylated, reduced, carboxamidomethylated, and maleylated
lysozyme-Sepharose. Purification was carried out separately from both the
soluble and particulate fractions. Whereas multiple and distinct enzyme
forms were obtained from each of these, little difference could be detected
between the behavior of the "soluble" enzyme subtypes and their
"particulate" counterparts. The major subtypes were purified to apparent
homogeneity with an approximately 23,000-fold enrichment and 10% yield from
the soluble fraction and a 4,300-fold enrichment and 13% yield from the
particulate fraction. Both samples migrated as bands of 35 kDa on sodium
dodecyl sulfate-polyacrylamide gel electrophoresis and had specific
activities of approximately 45,000 nmol of Pi released min- 1 mg-1, at
least 2-3-fold higher than that of the type 1 and 2A serine/threonine
phosphatases. The level of protein-tyrosine- phosphatases in the soluble
fraction of human placenta (2,000 units/g of protein) was approximately the
same as protein-serine/threonine- phosphatases 1 and 2A in skeletal muscle.
Purification of the major protein-tyrosine-phosphatases of human placenta
Department of Biochemistry, University of Washington, Seattle 98195.
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