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KMID : 0380219940270030230
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 3 p.230 ~ p.234
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Biochemical Properties of Human Organ-Specific Acid Phosphatase Isoenzymes
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Abstract
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Abstract:
@EN Four acid phosphatases (AcP) were newly purified to homogeneity from human lung, spleen, kidney, and bladder using affinity chromatography on L9+)-tartrate, an inhibitor of AcP. The biochemical properties, of these 4 phosphatases were
compared
with
the properties of phosphatase isolated from human prostate. All had a similar molecular weight of approximately 100 kDa, and exhibited maximum enzymic activity at pH 5.5 to 6.0. These acid phosphatases from the human lung, spleen, kidney, and
bladder
had similar substrate affinities toward several phospholmonoester substrates, and exhibited highest reactivities toward p-nitrophenyl phosphate, among the substrates examined. The AcP of the prostate had highest affinity toward a-naphthyl
phosphate.
Phosphotyrosine phosphatase activity on 32P-Tyr-labelled phosphopeptide substrates was demonstrated primarily by the AcP of the prostate. Although all AcP isoenzymes were inhibited to a similar extent by L(+)-tartrate, Fe3-, and fluoride, the AcP
of the
prostate was more sensitive to inhibition by Ca2, Ba2, La2, and ethanol than the other AcP isoenzymes. The amino acid compositions of lung, spleen, kidney, nad bladder AcPs were almost identical, but were different from the amino acid composition
of
prostatic AcP. These results suggest that the acid phosphatases of the human lung, spleen, kidney, and bladder are products of the same gene, and are protein molecules distinct from the acid phosphatase of the human prostate.
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