Proteins specified by herpes simplex virus. X. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels

D Wade Gibson, B. Roizman

Research output: Contribution to journalArticle

Abstract

Analyses of the structural proteins of herpes simplex virions and of capsids containing viral DNA (B capsids), after electrophoresis in polyacrylamide gels, revealed considerable variability in their properties with respect to : (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB protein complex at different wavelengths, (iii) relative efficiency with which 14C amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate polyacrylamide gels.

Original languageEnglish (US)
Pages (from-to)155-165
Number of pages11
JournalJournal of Virology
Volume13
Issue number1
StatePublished - 1974
Externally publishedYes

Fingerprint

herpes simplex
radiolabeling
capsid
Capsid
Capsid Proteins
Simplexvirus
polyacrylamide
virion
Virion
gels
Staining and Labeling
viruses
Herpes Simplex
Proteins
proteins
structural proteins
Viral DNA
sodium dodecyl sulfate
Sodium Dodecyl Sulfate
absorbance

ASJC Scopus subject areas

  • Immunology

Cite this

@article{5e034491682648fba4e664c74c658c78,
title = "Proteins specified by herpes simplex virus. X. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels",
abstract = "Analyses of the structural proteins of herpes simplex virions and of capsids containing viral DNA (B capsids), after electrophoresis in polyacrylamide gels, revealed considerable variability in their properties with respect to : (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB protein complex at different wavelengths, (iii) relative efficiency with which 14C amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate polyacrylamide gels.",
author = "Gibson, {D Wade} and B. Roizman",
year = "1974",
language = "English (US)",
volume = "13",
pages = "155--165",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "1",

}

TY - JOUR

T1 - Proteins specified by herpes simplex virus. X. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels

AU - Gibson, D Wade

AU - Roizman, B.

PY - 1974

Y1 - 1974

N2 - Analyses of the structural proteins of herpes simplex virions and of capsids containing viral DNA (B capsids), after electrophoresis in polyacrylamide gels, revealed considerable variability in their properties with respect to : (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB protein complex at different wavelengths, (iii) relative efficiency with which 14C amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate polyacrylamide gels.

AB - Analyses of the structural proteins of herpes simplex virions and of capsids containing viral DNA (B capsids), after electrophoresis in polyacrylamide gels, revealed considerable variability in their properties with respect to : (i) retention of Coomassie brilliant blue (CBB) and fast green stains during destaining, (ii) relative optical absorbance of the CBB protein complex at different wavelengths, (iii) relative efficiency with which 14C amino acids are incorporated during early and late periods of the infection cycle, and (iv) capacity to be phosphorylated in vivo. In addition, it was found that protein 22a of B capsids, which does not have an electrophoretically identical counterpart in virions, shares a relatively unique set of staining and radiolabeling properties with virion protein 22, which has a slightly more rapid electrophoretic mobility in sodium dodecyl sulfate polyacrylamide gels.

UR - http://www.scopus.com/inward/record.url?scp=0015948224&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015948224&partnerID=8YFLogxK

M3 - Article

C2 - 4129836

AN - SCOPUS:0015948224

VL - 13

SP - 155

EP - 165

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 1

ER -