Aminopeptidases of the rat prostatic complex and seminal vesicles: separation by gel filtration and chromatofocusing.
Aminopeptidases hydrolysing L-alanine-beta-naphthylamide (AlaNA), L-arginine-beta-naphthylamide (ArgNA) and L-leucine-beta-napthylamide (LeuNA) were studied in homogenate and after fractionation (gel filtration, chromatofocusing) of various parts of the rat prostatic complex (ventral lobe, VP; lateral lobe, LP; posterior lobe, PP; coagulating gland, CG) and seminal vesicles (VS). Marked differences were observed in the hydrolysis rates of these substrates in the various tissues studied. After fractionation up to seven activities were separated with differences in pH-optima, pI-values, molecular weights, substrate preferences and modifier characteristics. The number of enzyme activities characteristically varied between the tissues studied. Depending on the enzyme pattern in each part the differences in hydrolysis rates of the three substrates became apparent.
D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002850:Chromatography, Gel; D008297:Male; D011467:Prostate / Q000033:anatomy & histology / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D012669:Seminal Vesicles / Q000201:enzymology*; D013379:Substrate Specificity; D014018:Tissue Distribution
D000626:Aminopeptidases