Structure and function of a novel coliphage-associated sialidase

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

Research output: Contribution to journalArticlepeer-review

24 Citations (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.

Original languageEnglish
Pages (from-to)333-337
Number of pages5
JournalFEMS Microbiology Letters
Issue number2
Publication statusPublished - 2000 Jan 15


  • Coliphage
  • Disulfide bond
  • Electron micrograph
  • Sialidase
  • Tail plate


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