Purification, Properties, and N-Terminal Amino Acid Sequences of Guar Gum-degrading Enzyme from<i>Bacillus circulans</i>K-l

書誌事項

タイトル別名
  • Purification, Properties, and N-Terminal Amino Acid Sequences of Guar Gum-degrading Enzyme from Bacillus circulans K-1.
  • Purification Properties and N Terminal

この論文をさがす

説明

A guar gum-degrading enzyme of the newly isolated Bacillus circulans K-1 was purified to an electrophoretically homogeneous state. The molecular weight of the purified enzyme was 62, 000 by SDS-PAGE. The purified enzyme was separated into at least six isozymes by isoelectric focusing and the pI of these isozymes were 5.4, 5.5, 5.6, 5.8, 6.0, and 6.2, respectively. The N-terminal amino acid sequences of the typical three of these proteins were all the same, Ala-Ser-Gly-Phe-Tyr-Val-Ser-Gly-Thr-Lys-Leu-Leu-Asp-Ala-Thr-Gly-Gln-Pro-Phe-Val-Met-Arg. The enzyme was most active at pH 6.9 and at 64°C. The enzyme was activated slightly by Al3+ and inhibited strongly by Sn2+ and Zn2+, N-bromosuccinimide, 2-mer-captoethanol, and ethylenediamine-tetraacetic acid.

収録刊行物

被引用文献 (2)*注記

もっと見る

参考文献 (23)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ