Structure and function of a novel coliphage-associated sialidase.
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.
Machida
Y
Y
Department of Biotechnology, Graduate School of Bioengineering, Nagoya University, Chikusa-ku, Nagoya, Japan.
Miyake
K
K
Hattori
K
K
Yamamoto
S
S
Kawase
M
M
Iijima
S
S
D002458:Cell Fractionation; D003090:Coliphages / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000821:virology; D016253:Microscopy, Immunoelectron; D009439:Neuraminidase / Q000737:chemistry* / Q000378:metabolism*
D004220:Disulfides; D009439:Neuraminidase