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 language | English (US) |
|---|---|
| Pages (from-to) | 155-165 |
| Number of pages | 11 |
| Journal | Journal of Virology |
| Volume | 13 |
| Issue number | 1 |
| State | Published - 1974 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
Proteins specified by herpes simplex virus. X. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels. / Gibson, D Wade; Roizman, B.
In: Journal of Virology, Vol. 13, No. 1, 1974, p. 155-165.Research output: Contribution to journal › Article
}
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.
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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 -