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J. Biochem, 1967, Vol. 62, No. 3 353-363
© 1967 Japanese Biochemical Society

research-article

A Neutral Proteinase from Streptomycea naraensis

I. Purification and Some Properties

AKIRA HIRAMATSU

From the Laboratory of Biochemistry, Faculty of Agriculture, Ibaraki University Ami, Ibaraki

1. A neutral proteinase was isolated from the culture filtrate of Streptomyces naraensis by fractionation with acetone and subsequent chro-matography on columns of Amberlite CG-50 and DEAE-cellulose.

The purified proteinase was nearly homogeneous by zone electro-phoresis on a starch grain block and free-boundary electrophoresis, and it was purified about 130-fold. The purified enzyme preparation was shown to be free from carboxypeptidase and aminopeptidase activities by incubation with synthetic peptides.

2. The pH and the thermal stabilities increased remarkably on addition of calcium ion. During chromatographic purification, the addition of calcium ion was required.

3. The maximum activity of the neutral proteinase was obtained at pH 7.5 and 40°, and the activity was inhibited by the addition of the metal-chelating reagents and heavy metal ions.

4. No metal ion activated the enzyme activity. The activity of enzyme which had been inactivated with EDTA could be restored almost completely by the addition of zinc, but not calcium ion.


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