Some physico-chemical properties of the rigid form of the Sendai virus nucleocapsid.
The effect of some dissociation agents (SDS, beta-mercaptoethanol, urea, EDTA) on the rigid form of the Sendai virus nucleocapsid was studied. Polyacrylamide gel electrophoresis in the presence of lytic mixture (1% SDS, 2% beta-mercaptoethanol, 5 M urea, for 2 min at 100 degrees C) revealed two types of polypeptide subunits (mol. wts. 46,000 and 14,000), as well as the dissociation in the presence of 0.1% SDS only. The EDTA treatment leads to a disorganization of the protein part (10(-2) M) or of the nucleocapsid structure (5 x 10(-2) M).
Repanovici
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Stefan S. Nicolau Institute of Virology, Bucharest, Romania.
Hristova
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Popa
L M
LM
D002213:Capsid / Q000032:analysis / Q000187:drug effects / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human / Q000032:analysis / Q000187:drug effects / Q000302:isolation & purification*; D010455:Peptides / Q000032:analysis; D014758:Viral Core Proteins / Q000032:analysis / Q000187:drug effects / Q000302:isolation & purification*
D010455:Peptides; D014758:Viral Core Proteins