Purification and assays of tachycitin

研究成果: 書籍/レポート タイプへの寄稿

抄録

An antimicrobial peptide tachycitin (73 amino acids) is purified by steps of chromatography, including Sephadex G-50 and S Sepharose FF, from the acid extract of hemocyte debris of horseshoe crabs. Tachycitin is present in monomer form in solution, revealed by ultracentrifugation analysis. Tachycitin exhibits bacterial agglutination activity and inhibits the growth of both Gram-negative bacteria, Gram-positive bacteria, and fungus Candida albicans. Interestingly, tachycitin shows synergistic antimicrobial activity in corporation with another antimicrobial peptide, big defensin. Tachycitin shows a specific binding activity to chitin but not to cellulose, mannan, xylan, and laminarin. Tachycitin is composed of the N-terminal three-stranded β-sheet and the C-terminal two-stranded β-sheet following a short helical turn, and the C-terminal structural motif shares a significant structural similarity with the chitin-binding domain derived from a plant chitin-binding protein, hevein.

本文言語英語
ホスト出版物のタイトルMethods in Molecular Biology
出版社Humana Press Inc.
ページ317-323
ページ数7
DOI
出版ステータス出版済み - 2020

出版物シリーズ

名前Methods in Molecular Biology
2132
ISSN(印刷版)1064-3745
ISSN(電子版)1940-6029

!!!All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 遺伝学

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