Purification and characterization of a phosphotyrosyl-protein phosphatase from wheat seedlings.

Biochimica Et Biophysica Acta
H F Cheng, M Tao

Abstract

A neutral phosphatase which catalyzes the hydrolysis of p-nitrophenylphosphate has been purified to homogeneity from wheat seedlings. The enzyme is a monomeric glycoprotein exhibiting a molecular weight of 35,000, frictional ratio of 1.22, Stokes' radius of 260 nm, and sedimentation coefficient of 3.2 S. That the enzyme is a glycoprotein is surmised from its chromatographic property on Concanavalin A-Sepharose column. An examination of the substrate specificity indicates that the enzyme exhibits a preference for phosphotyrosine over a number of phosphocompounds, including p-nitrophenylphosphate and several glycolytic intermediates. Both phosphoserine and phosphothreonine are not hydrolyzed by the enzyme. The phosphatase activity is not affected by high concentrations of chelating agents and does not require metal ions. Molybdate, orthovanadate, Zn2+, and Hg2+ are all potent inhibitors of the phosphatase activity. The ability of the phosphatase to dephosphorylate protein phosphotyrosine has been investigated. [32P-Tyr]poly(Glu,Tyr)n, [32P-Tyr]alkylated bovine serum albumin, [32P-Tyr]angiotensin-I, and [32P-Tyr]band 3 (from human erythrocyte) are all substrates of the phosphatase. On the other hand, the enzyme has no activity tow...Continue Reading

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Citations

Jun 1, 1996·Annual Review of Plant Physiology and Plant Molecular Biology·Robert D. Smith, John C. Walker
Oct 17, 2012·The Journal of Biological Chemistry·Minjung ChaeGeorge M Carman
Sep 16, 1996·FEBS Letters·D SommerP S Song
Dec 15, 2020·International Journal of Biological Macromolecules·Umber ZamanAnwar Iqbal
Jul 1, 2001·The New Phytologist·Sheng LuanRajeev Gupta
Sep 23, 1992·Biochimica Et Biophysica Acta·G M Polya, R E Wettenhall
Mar 16, 1992·Biochimica Et Biophysica Acta·I JagiełłoG Muszyńska
Aug 1, 1991·Archives of Biochemistry and Biophysics·P P Waymack, R L Van Etten

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