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- W2056214920 abstract "Using [32P]P-Tyr-IgG and [32P]P-Tyr-casein phosphorylated by pp60v-src as substrates, studies on the phosphotyrosyl-protein phosphatase activity in human prostate gland indicate that it is associated with prostatic acid phosphatase. Evidence to support this conclusion include the following: (a) these two enzymatic activities co-purify to apparent homogeneity; (b) they co-migrated on polyacrylamide gel electrophoresis, ion-exchange and gel filtration chromatographies; (c) the exhibit identical thermostability; and (d) the phosphotyrosyl-protein phosphatase activity is sensitive to inhibition by p-nitrophenyl phosphate and by several classical inhibitors of prostatic acid phosphatase including l(+)-tartrate, molybdate, vanadate and NaF. The purified enzyme exhibits high specificity towards phosphotyrosyl-proteins with little activity towards several phosphoseryl-proteins and phosphothreonyl-proteins examined. The present findings indicate that prostatic acid phosphatase may function in vivo as a phosphotyrosyl-protein phosphatase." @default.
- W2056214920 created "2016-06-24" @default.
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- W2056214920 date "1984-01-01" @default.
- W2056214920 modified "2023-09-26" @default.
- W2056214920 title "A phosphotyrosyl-protein phosphatase activity associated with acid phosphatase from human prostate gland" @default.
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- W2056214920 doi "https://doi.org/10.1111/j.1432-1033.1984.tb07879.x" @default.
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