TY - JOUR
T1 - The polypeptides of adenovirus. II. Soluble proteins, cores, top components and the structure of the virion
AU - Maizel, Jacob V.
AU - White, David O.
AU - Scharff, Matthew D.
N1 - Funding Information:
1 This work was supported by NIH grants AI 4153 and 5231, NSF grants 4751 and GB 6364X, and American Cancer Society grant E 379. 2 Recipient of U.S.P.H.S. Career Development Award. 3 Supported by a Research Fellowship from the Damon Runyon Memorial Fund for Cancer Research. Present address: Department of Microbiology, University of Melbourne, Parkville, N.2, Victoria, Australia.
PY - 1968/9
Y1 - 1968/9
N2 - The adenovirion has been shown to have a much more complex structure than was previously assumed. Eight different types of polypeptides have been assigned a place in the particle. Three are present in an outer capsid, three in an inner core, and two others in association with hexons. The hexon capsomere is composed of about three molecules of a single type of peptide of molecular weight (MW) 120,000 which comprises about 50% of the total virion protein. Groups of such capsomeres, released from the virion by 5 M urea, are found to be associated with two minor polypeptides, each of MW 13,000. The penton-base is composed of a single type of peptide of MW 70,000, and the fiber is composed of another peptide of MW 62,000. The internal core released by treatment of the virion with 5 M urea, contains the viral DNA in association with three arginine-rich peptides of MW 44,000, 24,000, and 24,000, comprising some 20% of the total virion protein. The same three peptides are relatively lacking in the "empty" capsids found as the "top components" of cesium chloride gradients of crude virus preparations.
AB - The adenovirion has been shown to have a much more complex structure than was previously assumed. Eight different types of polypeptides have been assigned a place in the particle. Three are present in an outer capsid, three in an inner core, and two others in association with hexons. The hexon capsomere is composed of about three molecules of a single type of peptide of molecular weight (MW) 120,000 which comprises about 50% of the total virion protein. Groups of such capsomeres, released from the virion by 5 M urea, are found to be associated with two minor polypeptides, each of MW 13,000. The penton-base is composed of a single type of peptide of MW 70,000, and the fiber is composed of another peptide of MW 62,000. The internal core released by treatment of the virion with 5 M urea, contains the viral DNA in association with three arginine-rich peptides of MW 44,000, 24,000, and 24,000, comprising some 20% of the total virion protein. The same three peptides are relatively lacking in the "empty" capsids found as the "top components" of cesium chloride gradients of crude virus preparations.
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U2 - 10.1016/0042-6822(68)90122-0
DO - 10.1016/0042-6822(68)90122-0
M3 - Article
C2 - 5669983
AN - SCOPUS:0014330677
SN - 0042-6822
VL - 36
SP - 126
EP - 136
JO - Virology
JF - Virology
IS - 1
ER -