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Biochemical nature of the prostate‐associated antigen identified by the monoclonal antibody, KR‐P8
Author(s) -
Raynor Robert H.,
Hazra Tapan A.,
Moncure Charles W.,
Mohanakumar T.
Publication year - 1986
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.2990090106
Subject(s) - antigen , monoclonal antibody , antigenicity , microbiology and biotechnology , epitope , prostate specific antigen , biology , prostate , antibody , agglutinin , concanavalin a , trypsin , biochemistry , chemistry , immunology , lectin , in vitro , enzyme , cancer , genetics
The KR‐P8 monoclonal antibody identifies an organ‐specific antigen that is associated with normal as well as malignant specimens of human prostate tissue. The antigen is secreted by cells of the prostate and is present in samples of seminal plasma. Data presented here describe the biochemical nature of the antigen that is recognized by KR‐P8 as it occurs in seminal plasma and in extracts prepared from cells of the prostate tumor line, PC3. Antigen contained in seminal plasma migrated as a broad band on SDS‐polyacrylamide gels in the molecular weight range of 48,000–75,000 d. A similar pattern was observed for antigen prepared from detergent extracts of PC3 cells. The antigen was found to be sensitive to treatment with trypsin and chymotrypsin and the contribution of carbohydrate residues to the structure of the molecule was shown by studies that demonstrated binding of the antigen to Concanavalin A and Soybean Agglutinin lectins. Loss of antigenicity subsequent to periodate oxidation suggested that carbohydrate units are involved in the recognition site for KR‐P8 on the antigen.