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, Wade
N1 - Funding Information:
I thank Dr. W’alter Eckhart. in whose laboratory these studies were done. for his advice and support; Drs. Gernot Walter, Theodore Friedmann, and Gary David for many helpful suggestions during the course of these experiments; and Mary Anne Hutchinson for her expert technical assistance. The Sepharose bead-bound lactoperoxidase was generously prov-ided by Dr. Gary David. This research was supported by Research Grant CA 13884 from the National Cancer Institute, and by a postdoctoral fellowship from the Damon Runyon Memorial Fund for Cancer Research.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1974/12
Y1 - 1974/12
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 -