Carbohydrate removal fails to eliminate the heterogeneity of human prostatic acid phosphatase

Clinica Chimica Acta; International Journal of Clinical Chemistry
M F MorrisR L Van Etten

Abstract

Human prostatic acid phosphatase is known to display considerable charge heterogeneity upon isoelectric focusing. The structural basis of this heterogeneity is not known, although it has been widely attributed to variations in the nature of the carbohydrate chains or to substituents on the carbohydrate chains of the glycoprotein. In this study, the role of the carbohydrate chains in the charge heterogeneity of the protein was examined. First, sialic acid residues were removed by treatment of the acid phosphatase with neuraminidase. The desialo enzyme was fractionated and purified by L-tartramic acid affinity chromatography. Then, after the protein oligosaccharide linkages were made accessible by the presence of NP-40 or by denaturing the protein, the protein was completely deglycosylated by endo-beta-N-acetylglucosaminidase F at pH 4.5 and 9.3. Two discrete intermediates were clearly resolved by SDS gel electrophoresis during the deglycosylation of the denatured protein at pH 9.3, indicating the existence of three sites of glycosylation on the protein. Peptide mixtures were obtained by digestion of carboxymethylated and citraconylated derivatives of the enzyme with trypsin and the glycopeptides were isolated. The amino acid com...Continue Reading

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Citations

Sep 1, 1995·International Journal of Urology : Official Journal of the Japanese Urological Association·T YoshikiO Yoshida
Jan 1, 1995·Critical Reviews in Clinical Laboratory Sciences·D W MossD B Wile
Jan 1, 1990·Andrologia·P A Abrahamsson, H Lilja

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