A Neutral Proteinase from <i>Streptomyces naraensis</i>:III. An Improved Purification and Some Physicochemical Properties

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  • HIRAMATSU Akira
    The Laboratory of Biochemistry, Faculty of Agriculture, Ibaraki University
  • OUCHI Takeshi
    The Laboratory of Biochemistry, Faculty of Agriculture, Ibaraki University

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説明

1. A neutral proteinase [EC 3. 4. 4 group] from Streptomyces naraensis was purified 100 to 130-fold by a modified method using gel filtration on Sephadex G-100 and column chromatography on DEAE-cellulose. The preparation thus obtained was homogeneous in ultracentrifugation, in free-boundary electrophoresis, in disc electro-phoresis and on column chromatographies.<br> 2. The molecular weight was 37, 100 using the Scherage-Mandelkern formula, based upon the values of the sedimentation coefficient (so20, W=3.31S), the intrinsic viscosity ([η]=0.0288 dl•g-1), and partial specific volume (_??_=0.744ml•g-1). Its isoelectric point was pH 4.2.<br> 3. The chemical composition of the enzyme was as follows: nitrogen 16.49 percent, zinc 0.176 percent, and neutral sugar (glucose) 1.86 percent with the complete absence of hexosamine and sialic acid. Thus, the neutral proteinase contains 1g atom of zinc per mole of the enzyme and the carbohydrate analyses suggest that the neutral proteinase is a glycoprotein.<br> 4. From the molecular weight and the amino acid content, the following amino acid composition was calculated for the enzyme; Asp47, Glu14, GIy50, Ala41, Val20, Leu18, Ile12, Ser31, Thr39, Cys2, Met2, Pro11, Phe11, Tyr23, Trp4, His10, Lys13, Arg9, (amide-NH2)18. There are 357 amino acid residues per mole of the enzyme.

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