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Comparison of the properties of NTPase in avian myeloblastosis virus and myeloblasts

Technical Report ·
OSTI ID:6251304
Subviral particles containing viral nucleoside triphosphatase (NTPase) activity were isolated from sucrose density gradients of avian myeloblastosis virus (AMV) exposed to 1% cholate at 0/sup 0/ for 2 hr. The NTPase fraction contained about 10% of the protein added to the gradients; the remainder of the protein was soluble, demonstrating that virus cores were disrupted. Specific activity of the NTPase in the isolated preparation was threefold higher than that of AMV and sevenfold higher than cholate-exposed AMV. Gel electrophoresis in sodium dodecyl sulfate revealed that the particles contained at least nine proteins, including the major and minor viral glycoproteins; only traces of core proteins were present. Electron microscopy of negative-stained preparations demonstrated that the material was, for the most part, aggregates of AMV-sized vesicles, suggesting that the preparation consisted of isolated virus envelopes. Intact myeloblasts exhibited the NTPase activity on their external surfaces. The specific activity of a membrane fraction isolated from these cells was about six times less than that of a virion and 25 times less than that of a viral envelope fraction. The data suggest that the nascent envelope accumulates the enzyme during its formation in the cell membrane. 31 references, 6 figures, 4 tables.
Research Organization:
Pacific Northwest Lab., Richland, WA (USA)
DOE Contract Number:
AC06-76RL01830
OSTI ID:
6251304
Report Number(s):
PNL-SA-10809; ON: DE85006085
Country of Publication:
United States
Language:
English

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