Human seminal proteinase and prostate-specific antigen are the same protein.
Human seminal proteinase and prostate-specific antigen (PSA) were each isolated from human seminal fluid and compared. Both are glycoproteins of 32-34 kDa with protease activities. Based on some physicochemical,enzymatic and immunological properties,it is concluded that these proteins are in fact identical. The protein exhibits properties similar to kallikrein-like serine protease, trypsin,chymotrypsin and thiol acid protease. Tests of the activity of the enzyme against some potential natural and synthetic substrates showed that bovine serum albumin was more readily hydrolysed than casein. The results of this study should be useful in purifying and assaying this protein. Based on published studies and the present results,the broad proteolytic specificity of human seminal proteinase suggests a role for this protein in several physiological functions.
Edward A Doisy Department of Biochemistry and Molecular Biology, St Louis University School of Medicine, St Louis, MO 63104, USA.
Abdul
A
Waheed
Md Imtaiyaz
MI
Hassan
Robert L Van
RL
Etten
Faizan
F
Ahmad
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism*; D010449:Peptide Mapping; D017430:Prostate-Specific Antigen / Q000378:metabolism*; D012661:Semen / Q000201:enzymology*
D010447:Peptide Hydrolases; D017430:Prostate-Specific Antigen