Basic arginine esterase from human seminal plasma: purification and some properties.
Basic arginine esterase (amidase) with a specific activity of 3.2 mumol N-alpha-tosyl-L-arginine methyl ester (Tos-Arg-Me) esterolysis per A280 was purified about 230-fold from a CM-cellulose absorbed preparation of human seminal plasma. The purified enzyme was a single band with an apparent molecular weight of 3.4-4.1 x 10(4). The amidolytic activity of this enzyme was suppressed by aprotinin, soybean trypsin inhibitor (SBTI), leupeptin, and antipain, while alpha 1-antitrypsin, ovomucoid trypsin inhibitor (OTI), EDTA, and chymostatin had no or weak effect. This enzyme hydrolyzed synthetic basic amino acid derivatives and N-alpha-tosyl-glycyl-L-prolyl-arginine-p-nitroanilide (Tos-Gly-Pro-Arg-pNA) and N-alpha-tert-butyloxycarbonyl-L-leucyl-L-prolyl-L-arginine-p-nitroanilid e (Boc-Leu-Pro-Arg-pNA) were the best substrates. The enzymatic characteristics of present enzyme were clearly different from tissue kallikrein, acrosin, and seminin in human semen.
Kobayashi
T
T
First Department of Biochemistry, Meiji College of Pharmacy, Tokyo, Japan.
Park
J Y
JY
Matsuda
Y
Y
Hara
I
I
Kaneko
S
S
Oshio
S
S
Akihama
S
S
Fujimoto
Y
Y
D000595:Amino Acid Sequence; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D012661:Semen / Q000201:enzymology*; D016622:Silver Staining; D013379:Substrate Specificity
D009842:Oligopeptides; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases