Abstract
Examination of the protein components of highly purified polyoma virions by electrophoretic separation in SDS-polyacrylamide gels has revealed the presence of three previously undetected protein bands. Two of these, designated P3a and P4a, were not found in lysates of infected cells and may represent modified products of their respective doublet partners, P3b and P4b. The third, P6a, along with P5, P6b, and P7 are electrophoretically indistinguishable from protein bands present in the nuclear fraction of both infected and uninfected cells, and represent the virion counterparts of the host cell histones. Comparisons of the major nonhistone proteins, P2, P3, and P4, by tryptic peptide analyses have shown that P3 and P4 are closely related, but that P2 appears to be independently coded.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 319-336 |
| Number of pages | 18 |
| Journal | Virology |
| Volume | 62 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1974 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Virology
- Infectious Diseases
Cite this
Polyoma virus proteins : A description of the structural proteins of the virion based on polyacrylamide gel electrophoresis and peptide analysis. / Gibson, D Wade.
In: Virology, Vol. 62, No. 2, 1974, p. 319-336.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Polyoma virus proteins
T2 - A description of the structural proteins of the virion based on polyacrylamide gel electrophoresis and peptide analysis
AU - Gibson, D Wade
PY - 1974
Y1 - 1974
N2 - Examination of the protein components of highly purified polyoma virions by electrophoretic separation in SDS-polyacrylamide gels has revealed the presence of three previously undetected protein bands. Two of these, designated P3a and P4a, were not found in lysates of infected cells and may represent modified products of their respective doublet partners, P3b and P4b. The third, P6a, along with P5, P6b, and P7 are electrophoretically indistinguishable from protein bands present in the nuclear fraction of both infected and uninfected cells, and represent the virion counterparts of the host cell histones. Comparisons of the major nonhistone proteins, P2, P3, and P4, by tryptic peptide analyses have shown that P3 and P4 are closely related, but that P2 appears to be independently coded.
AB - Examination of the protein components of highly purified polyoma virions by electrophoretic separation in SDS-polyacrylamide gels has revealed the presence of three previously undetected protein bands. Two of these, designated P3a and P4a, were not found in lysates of infected cells and may represent modified products of their respective doublet partners, P3b and P4b. The third, P6a, along with P5, P6b, and P7 are electrophoretically indistinguishable from protein bands present in the nuclear fraction of both infected and uninfected cells, and represent the virion counterparts of the host cell histones. Comparisons of the major nonhistone proteins, P2, P3, and P4, by tryptic peptide analyses have shown that P3 and P4 are closely related, but that P2 appears to be independently coded.
UR - http://www.scopus.com/inward/record.url?scp=0016363043&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0016363043&partnerID=8YFLogxK
U2 - 10.1016/0042-6822(74)90395-X
DO - 10.1016/0042-6822(74)90395-X
M3 - Article
C2 - 4372784
AN - SCOPUS:0016363043
VL - 62
SP - 319
EP - 336
JO - Virology
JF - Virology
SN - 0042-6822
IS - 2
ER -