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Studies on the structural basis of the heterogeneity of human prostatic and seminal acid phosphatases
Author(s) -
Taga Eulazio M.,
Moore D. Lane,
Van Etten Robert L.
Publication year - 1983
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990040205
Subject(s) - prostatic acid phosphatase , isoelectric focusing , sialic acid , amino acid , neuraminidase , biochemistry , phosphatase , enzyme , acid phosphatase , prostate , isoelectric point , polyacrylamide gel electrophoresis , chemistry , electrophoresis , biology , cancer , genetics
We studied possible causes of the electrophoretic heterogcncity of the acid phosphatase (EC 3.1.3.2) purified by affinity chromatography from human prostate and human seminal fluid. The isoelectric focusing pattern in polyacrylamide gel shows numerous bands in the pH range 4.0–5.2 and 5.5–5.9. Treatment with neuraminidaae under conditions shown to cause complete removal of sialic acid does not abolish the observed heterogeneity. Although there is a change of the more acidic forms to ones having more basic pI values, at least 4 distinct bands remain. Structural differences at thr amino terminal end can be ruled out as the cause of the remaining electrophoretic heterogeneity. Lysine is shown to be the amino terminal amino acid for both the prostatic and seminal fluid enzymes. The bequences of the first 23 amino acids are shown to be identical for the prostatic and seminal fluid acid phosphatases. The functional enzyme contains no metal ion but it can be stoichiometrically inactivated by cupric ion.