発芽ダイズ種子カルボキシペプチダーゼ(第2報) : カルボキシペプチダーゼS<SUB>a</SUB>およびS<SUB>b</SUB>の安定性, 化学的および動力学的性質

DOI Web Site Web Site 被引用文献1件

書誌事項

タイトル別名
  • Carboxypeptidases from Germinating Soybeans. II. : Stability and Some Chemical and Kinetic Properties of Carboxypeptidases S<SUB>a</SUB> and S<SUB>b</SUB>
  • 発芽ダイズ種子カルボキシペプチダーゼー2-カルボキシペプチダーゼSaおよびSbの安定性,化学的および動力学的性質
  • ハツガ ダイズ シュシ カルボキシ ペプチダーゼ 2 カルボキシ ペプチダーゼ

この論文をさがす

抄録

Carboxypeptidase Sa was composed of 716 amino acid residues, 90 hexose residues (as galactose), and 31 hexosamine residues (as glucosamine) ; these were Trp14, Lys42, His15, Arg21, Asp77, Thr42, Ser60, Glu50, Pro34, Gly48, Ala57, Val50, Met6, Ile56, Leu93, Tyr22, and Phe34. Carboxypeptidase Sb was composed of 969 amino acid residues but was free from hexose and hexosamines ; these were Trp21, Lys62, His19, Arg35, Asp109, Thr49, Ser73, Glu84, Pro49, Gly88, Ala74, Gys (half)4, Val62, Met15, Ile49, Leu75, Tyr34, and Phe47. Carboxypeptidase Sa was stable in the pH range from 4.5 to 6.5 and in the temperature range from 0 to 50°, but carboxypeptidase Sb was quickly denatured at pH values below 5.0 or over 6.0. They were completely inhibited by the detergents, sodium dodecyl sulfate and cetyltrimethylammonium bromide, but not by Tween 80 or Triton X-100. The Km and Vmax values of carboxypeptidase Sa for the hydrolysis of Z-Glu-Phe were 0.16 M and 0.29 μmol/min/·mg, respectively, and those of carboxypeptidase Sb were 0.053 M and 11.36 μmol/min·mg, respectively.

収録刊行物

  • 薬学雑誌

    薬学雑誌 96 (12), 1421-1425, 1976

    公益社団法人 日本薬学会

被引用文献 (1)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ