Basic Arginine Esterase from Human Seminal Plasma: Purification and Some Properties

T. Kobayashi First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

J.-Y. Park First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

Y. Matsuda First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

I. Hara First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

S. Kaneko First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

S. Oshio First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

S. Akihama First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

Y. Fujimoto First Department of Biochemistry, Meiji College of Pharmacy, Nozawa, Setagaya-ku, Tokyo, 154, Japan; Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo, Japan; Department of Urology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, Japan; Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru-shi, Hokkaido, 047-02, Japan

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Abstract

Basic arginine esterase (amidase) with a specific activity of 3.2 μmol N-α-tosyl-L-arginine methyl ester (Tos-Arg-Me) esterolysis per A280 purified about 230-fold from a CM-cellulose adsorbed preparation of human seminal plasma. The purifed enzyme was a single band with an apparent molecular weight of 3.4–4.1 × 10⁴. The amidolytic activity of this enzyme was suppressed by aprotinin, soybean trypsin inhibitor (SBTI), leupeptin, and antipain, while α₁ - antitrypsin, ovomucoid trypsin inhibitor (OTI), EDTA, and chymostatin had no or weak effect. This enzyme hydrolyzed synthetic basic amino acid derivatives and N-α-tosyl-glycyl-L-prolyl-arginine-p-nitroanilide (Tos-Gly-Pro-Arg-pNA) and N-α-tert-butyloxycarbonyl-L-leucyl-L-prolyl-L-arginine-p-nitroanilide (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.

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Basic Arginine Esterase from Human Seminal Plasma: Purification and Some Properties

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Basic Arginine Esterase from Human Seminal Plasma: Purification and Some Properties

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