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FEMS Microbiol Lett. 2000 Jan 15;182(2):333-7.

Structure and function of a novel coliphage-associated sialidase.

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1
Department of Biotechnology, Graduate School of Bioengineering, Nagoya University, Chikusa-ku, Nagoya, Japan.

Abstract

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.

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