Structure and function of a novel coliphage-associated sialidase

Yuichi MacHida, Katsuhide Miyake, Kouji Hattori, Shin Yamamoto, Mitsuo Kawase, Shinji Iijima

研究成果: Article査読

21 被引用数 (Scopus)


A coliphage named 63D, isolated previously, associated sialidase as a component of phage particles. In order to localize the enzyme in phage particles, phages were partially destroyed by sonication, and the disrupted particles were size fractionated using a sucrose density gradient. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, enzyme assay and electron micrography of the fractions revealed the enzyme to be composed of four identical subunits with a molecular mass of 90 kDa, and the subunits were cross-linked by disulfide bonds. Electron micrographic observation indicated that six enzyme molecules were localized in a phage tail plate as a hexagonal array. Copyright (C) 2000 Federation of European Microbiological Societies.

ジャーナルFEMS Microbiology Letters
出版ステータスPublished - 2000 1 15

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

フィンガープリント 「Structure and function of a novel coliphage-associated sialidase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。