Comparison of adenoviral hexon polypeptides (monomers) and of native hexons (trimers) by SDS-polyacrylamide gel electrophoresis.
Purified hexons of 27 serotypes of human, simian, bovine and avian adenoviruses were analysed by SDS-PAGE. The apparent molecular weights of hexon polypeptides calculated by comparison with 5 non-hexon and 3 sequenced hexon polypeptide markers ranged from 98 kDa (for bovine adenovirus Ad bos7) to 118 kDa (for simian adenovirus Ad sim13; SV36). A stability of native hexon capsomers (trimers) in SDS at room temperature permitted us to resolve native (trimeric) hexon by SDS-PAGE and to distinguish them from denatured (monomeric) hexon polypeptides by electrophoretic mobilities. Hexon trimer bands with slow mobility in SDS-PAGE (unlike hexon monomer polypeptide bands) retained native hexon antigenicity as revealed by immunoblot analyses. Possible applications of simultaneous analyses of hexon trimers and monomers by SDS-PAGE are discussed.
Khilko
S N
SN
Research Institute for Agricultural Biotechnology, Moscow, USSR.
Kirasova
M A
MA
Kiseleva
E K
EK
Tikchonenko
T I
TI
D000256:Adenoviridae / Q000032:analysis* / Q000145:classification / Q000276:immunology; D000956:Antigens, Viral / Q000302:isolation & purification; D002213:Capsid / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D036022:Capsid Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008970:Molecular Weight; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate
D000956:Antigens, Viral; D036022:Capsid Proteins; C018315:hexon capsid protein, Adenovirus; D012967:Sodium Dodecyl Sulfate