title: Enzymatic action of basic arginine amidases in human seminal plasma.
abstract: Three basic arginine amidases with different affinities to lima bean trypsin inhibitor (LBTI) and aprotinin affinity columns were separated in the middle molecular weight (MMW) preparation obtained from Cellulofine GCL-2000 gel filtration of CM-cellulose adsorbed human seminal plasma and were tentatively called basic human seminal plasma arginine amidase-L (BHSAA-L, with affinity to LBTI), -A (BHSAA-A, with affinity to aprotinin), and -TH (BHSAA-TH, without affinity to either). Some enzymatic properties were measured, including Ki values of LBTI and human seminal plasma proteinase inhibitor (HSP-PI) toward present enzymes. The Ki values of LBTI toward BHSAA-L and -TH were lower than those of HSP-PI and no Ki values for LBTI toward BHSAA-L were observed. The Km values of BHSAA-L and -A to some tripeptidyl-p-nitroanilide substrates seemed relatively lower than that of BHSAA-TH.
mesh_terms: D000328:Adult; D000595:Amino Acid Sequence; D007611:Aprotinin / Q000032:analysis; D001120:Arginine / Q000378:metabolism*; D002846:Chromatography, Affinity; D004950:Esterases / Q000032:analysis; D006801:Humans; D007202:Indicators and Reagents; D007700:Kinetics; D008297:Male; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000032:analysis*; D010940:Plant Proteins; D011480:Protease Inhibitors / Q000032:analysis; D012661:Semen / Q000201:enzymology*
chemical_list: D007202:Indicators and Reagents; D010940:Plant Proteins; D011480:Protease Inhibitors; C025398:protease inhibitor protein, Phaseolus lunatus; D007611:Aprotinin; D001120:Arginine; D004950:Esterases; D010447:Peptide Hydrolases