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PMID: 221670 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2).

Journal of virology ·Vol. 29 ·No. 3 ·1979-03-00 ·Pages 1159-67

Sarmiento M, Spear PG

Abstract

The herpes simplex virus glycoprotein designated VP7(B2) is extracted from virions by nonionic detergent in the form of an oligomer, whereas the other detergent-soluble envelope proteins appear to be extracted as monomers. The subunits of the VP7(B2) oligomer cannot be dissociated by 2-mercaptoethanol and are also resistant to dissociation by a mixture of sodium dodecyl sulfate and 2-mercaptoethanol, except at elevated temperature. The oligomeric form of solubilized VP7(B2) appears to be predominantly dimeric, based on the sedimentation rats in sucrose gradients and the electrophoretic mobilities in sodium dodecyl sulfate-containing acrylamide gels of the undissociated and heat-dissociated forms of VP7(B2).

MeSH Terms
Glycoproteins/analysis Hot Temperature Mercaptoethanol/pharmacology Protein Conformation Simplexvirus/analysis,drug effects Sodium Dodecyl Sulfate/pharmacology Solubility Surface-Active Agents/pharmacology Viral Proteins/analysis
Chemicals
Glycoproteins Surface-Active Agents Viral Proteins Sodium Dodecyl Sulfate Mercaptoethanol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sarmiento M
Spear P G
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31 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1979-03-00
Pages
1159-67
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC353276
Subset
IM
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