Association of a ribonuclease with the purified influenza virus
作者:
D. J. S. Arora,
V. Pavilanis,
A. Soula,
P. Robert,
G. Croteau,
期刊:
Canadian Journal of Microbiology
(NRC Available online 1976)
卷期:
Volume 22,
issue 1
页码: 57-63
ISSN:0008-4166
年代: 1976
DOI:10.1139/m76-008
出版商: NRC Research Press
数据来源: NRC
摘要:
Purified influenza virus contains ribonuclease activity. The enzyme does not hydrolyze viral RNA but both 28 S and 18 S host cell RNA are degraded forming large (about 16 S) and small (about 5 S) fragments with the release of the acid-soluble material.It has an optimum temperature of 37 °C, requires no divalent ions, and is inhibited by 0.1 MEDTA and 1% SDS. Treatment with 4 Murea increases enzymatic activity considerably (42%) but is not a prerequisite for eliciting ribonuclease activity suggesting that the enzyme is probably located near the surface of the virus particle. Results show that the observed enzyme activity is virus-associated as no host cell protein is detectable in the purified virus.
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