Characteristics of partially purified prolidase and prolinase from the human prostate.
Both prolidase and prolinase from the human prostate were separated into two peaks by TSK DEAE-5PW chromatography. These peaks of prolidase isozymes I and II differed from each other in their responses to preincubation with Mn2+, their substrate specificity, optimal pH, and heat stability. The molecular weights of prolidases I and II were estimated to be 110,000 and 165,000, respectively, by gel filtration. Substrate specificity of prolinase peaks I and II was almost the same, but they differed in optimal pH and heat stability. The molecular weights of prolinases I and II were about 85,000 and 63,000, respectively. These results indicate that two isozymes of prolidase and of prolinase, which differ in various characteristics, are present in the human prostate.
Masuda
S
S
Department of Urology, Kochi Medical School, Japan.
Watanabe
H
H
Morioka
M
M
Fujita
Y
Y
Ageta
T
T
Kodama
H
H
D000368:Aged; D000369:Aged, 80 and over; D002851:Chromatography, High Pressure Liquid; D004150:Dipeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D008297:Male; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D011467:Prostate / Q000201:enzymology*; D013379:Substrate Specificity
D004151:Dipeptides; D007527:Isoenzymes; D008345:Manganese; D004150:Dipeptidases; C022454:prolyl dipeptidase; C022449:proline dipeptidase