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  • Title: Human prostatic acid phosphatase: purification, characterization, and optimization of conditions for radioimmunoassay.
    Author: McCarthy RC, Jakubowski HV, Markowitz H.
    Journal: Clin Chim Acta; 1983 Aug 31; 132(3):287-99. PubMed ID: 6193909.
    Abstract:
    Prostatic acid phosphatase was isolated from benign hypertrophic prostate tissue by ammonium sulfate precipitation and affinity chromatography procedures. The purified enzyme was characterized by two-dimensional gel electrophoresis and shown to have a cluster of protein spots with an apparent molecular weight of 48 000 at pI 5.9 to 6.3 in 9 mol/l urea. The specific activity of the purified enzyme was 723 and 659 U/mg protein with alpha-naphthyl phosphate at 30 degrees C and para-nitrophenyl phosphate at 37 degrees C respectively. An antibody to the purified enzyme was raised in rabbits and used in a radioimmunoassay (RIA). The use of a phosphate buffer, pH 6.6, and iodination of prostatic acid phosphatase (PAP) by the Bolton-Hunter procedure improved the precision of the assay when compared to RIA's using a phosphate buffer, pH 7.0 or 7.3, or PAP iodinated by a chloramine-T procedure. The former RIA displaced 50% of the tracer at 2 micrograms of enzyme per liter of serum. The between-run coefficient of variation for 11 assays ranged from 3.9-7.7% with serum at 1.3 to 5.6 micrograms PAP/l.
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