Home LiteratureArticle Details
PMID: 184330 Published · ppublish English Comparative Study Journal Article

Preferential phosphorylation of NP-protein of influenza A2 virus by virion-associated protein kinase.

Japanese journal of microbiology ·Vol. 20 ·No. 3 ·1976-06-00 ·Pages 227-32

Sugiyama K, Kamada T, Shimizu K, Watanabe Y

Abstract

Influenza A2 virions were found to contain protein kinase activity which was stimulated, like in other virion-associated kinases, with Mg++ and Nonidet-P 40 but not with cyclic AMP. The kinase phosphorylated only the NP-protein fraction of the influenza virions in the in vitro reaction. In contrast, none of the influenza virion proteins were phosphorylated significantly during the process of virus production in infected chorioallantoic membranes. The in vitro and in vivo phosphorylations of influenza viral proteins were compared with those of Sendai virus (HVJ).

MeSH Terms
Animals Chick Embryo Culture Techniques Cyclic AMP/pharmacology Extraembryonic Membranes Magnesium/pharmacology Parainfluenza Virus 1, Human/enzymology,metabolism Protein Kinases/metabolism Surface-Active Agents/pharmacology Viral Proteins/metabolism
Chemicals
Surface-Active Agents Viral Proteins Cyclic AMP Protein Kinases Magnesium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sugiyama K
Kamada T
Shimizu K
Watanabe Y
Article Info
Journal
Japanese journal of microbiology
Abbr.
Jpn J Microbiol
ISSN
0021-5139
Published
1976-06-00
Pages
227-32
Language
English
Region
Japan
NLM ID
0376565
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com