Comparison of the antigenic peptides between human prostatic and lysosomal acid phosphatases.
The relative antigenicity (capacity to bind antibodies raised against the intact prostatic acid phosphatase) of the selected peptides from human prostatic and lysosomal acid phosphatases was evaluated in a competitive assay. Both prostatic and lysosomal acid phosphatases were shown to possess similar antigenic determinants on both terminal regions, along with more similarity on NH2-terminal peptide than COOH-terminal site. At least one additional antigenic site is present at the internal region of prostatic acid phosphatase, since the mixture of both amino- and carboxyl-terminal peptides exhibited only 70% inhibition.
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Department of Diagnostic Immunology Research and Biochemistry, Roswell Park Memorial Institute, Buffalo, New York 14263.
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D000135:Acid Phosphatase / Q000737:chemistry / Q000276:immunology*; D000595:Amino Acid Sequence; D001666:Binding Sites, Antibody; D000939:Epitopes / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D006801:Humans; D008247:Lysosomes / Q000201:enzymology*; D046911:Macromolecular Substances; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology; D011467:Prostate / Q000201:enzymology*; D014357:Trypsin
D000939:Epitopes; D046911:Macromolecular Substances; D010446:Peptide Fragments; D000135:Acid Phosphatase; D014357:Trypsin