volume 16, issue 2, P99-103 1994
DOI: 10.1016/0141-0229(94)90070-1
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Youhei Yamagata, Kyoko Arakawa, Megumi Yamaguchi, Mikihiko Kobayashi, Eiji Ichishima

Abstract: A serine alkaline proteinase (EC 3.4.21.62) from Bacillus sp. (ALPase I) was modified with the 2,4-dialdehyde derivative of clinical dextran (dialdehyde dextran). The modified preparation was purified using an ion-exchange column and gel filtration. The modified enzyme contained 75% carbohydrate by weight. The isoelectric point (pI) of ALPase I was converted from 8.2 to approximately 5.0 by this modification. The specific activity of the dextran-modified ALPase I was 56% of that of the native enzyme when milk …

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