Biochemical properties of human prostatic acid phosphatase.

@article{Lam1973BiochemicalPO,
  title={Biochemical properties of human prostatic acid phosphatase.},
  author={Kent W. K. Lam and Oliver Li and C Y Li and Lung T. Yam},
  journal={Clinical chemistry},
  year={1973},
  volume={19 5},
  pages={483-7}
}
The electrophoretic pattern (in polyacrylamide gel) for acid phosphatases in the prostate gland was compared with that for other tissues. lsoenzyme 2 predominates in the prostate. The isoenzyme was isolated from the prostate and its biochemical properties were compared with those of acid phosphatases isolated from spleen. lsoenzyme 2 has a molecular weight of about 100,000. Its optimum pH is between 5 and 7, unlike other lysosomal enzymes. Its substrate specificity is not very much different… CONTINUE READING

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