Detergent-inhibited, heat-labile nucleoside triphosphatase in cores of avian myeloblastosis virus.

AUTOR(ES)

Jensen, K F

RESUMO

Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.

Documentos Relacionados

• Inhibition of virion-associated reverse transcription by nucleoside triphosphatase in avian myeloblastosis virus.
• Serotype-related differences in production and type of heat-labile hemolysin and heat-labile cytotoxin of Actinobacillus (Haemophilus) pleuropneumoniae.
• Heat-labile Enzymes in a Psychrophilic Bacterium
• Molecular organization of heat-labile enterotoxin genes originating in Escherichia coli of human origin and construction of heat-labile toxoid-producing strains.
• Serum heat-labile opsonins in systemic lupus erythematosus.