枯草芽孢杆菌丙氨酸脱氢酶的纯化及化学性质研究

Akira Yoshida, Ernst Freese
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引用次数: 60

摘要

1.1. 枯草芽孢杆菌丙氨酸脱氢酶(l -丙氨酸:NAD氧化还原酶(脱氨),EC1.4.1.1。经磷酸钙凝胶、DEAE-Sephadex和Ecteola-cellulose柱层析纯化;它以结晶形式得到。沉积模式表明是一种均质制剂。无限稀释下的沉淀常数为8.8 s,沉淀平衡法估算的分子量为228 000.3.3。氨基酸分析得到氨基酸残基比值:Asp, 43;34岁的刺;Ser 20;Glu, 51;专业,25岁;通用电气,51;阿拉巴马州,65;CySH 2;瓦尔,49个;满足,11;iLeu, 28日;低浓缩铀,42岁;酪氨酸,15;板式换热器,7;试,1;赖氨酸,28日;他,9;参数,14。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Purification and chemical characterization of alanine dehydrogenase of Bacillus subtilis

  • 1.

    1. Bacillus subtilis alanine dehydrogenase (L-alanine: NAD oxidoreductase (deaminating), EC1.4.1.1. has been purified by column chromatography using calcium phosphate gel, DEAE-Sephadex and Ecteola-cellulose; it has been obtained in crystalline form.

  • 2.

    2. The sedimentation pattern indicated a homogenous preparation. The sedimentation constant at infinite dilution was 8.8 S. The molecular weight estimated by the sedimentation equilibrium method was 228 000.

  • 3.

    3. Amino acid analysis gave the following ratios of amino acid residues: Asp, 43; Thr, 34; Ser, 20; Glu, 51; Pro, 25; Gly, 51; Ala, 65; CySH, 2; Val, 49; Met, 11; iLeu, 28; Leu, 42; Tyr, 15; Phe, 7; Try, 1; Lys, 28; His, 9; Arg, 14.

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