Open AccessStructure and function of a novel coliphage‐associated sialidase
Author(s) -
Machida Yuichi,
Miyake Katsuhide,
Hattori Kouji,
Yamamoto Shin,
Kawase Mitsuo,
Iijima Shinji
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb08917.x
Subject(s) - coliphage , molecular mass , enzyme , gel electrophoresis , sodium dodecyl sulfate , chemistry , sialidase , polyacrylamide gel electrophoresis , electrophoresis , biochemistry , biology , bacteriophage , escherichia coli , neuraminidase , gene
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.