Characterization of the adenosine triphosphatase of avian myeloblastosis virus. |
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| Authors: | R P Schneider G S Beaudreau |
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| Institution: | Biology Department, Pacific Northwest Laboratory, Richland, Washington 99352 U.S.A.;Department of Agricultural Chemistry, Oregon State University, Corvallis, Oregon 97331 U.S.A. |
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| Abstract: | The ATPase of avian myeloblastosis virus (AMV) is not a recognizable cellular enzyme. It hydrolyzes ATP, GTP, ITP, UTP, and dCTP at equal rates, is inhibited by high concentrations of dithiothreitol, and is partially inhibited by 1 × 10?5mp-chloromercuribenzoic acid (PCMB) and p-chloromercuribenzene sulfonate acid (PCMBS). The inhibition by the mercurials is reversed by increasing the concentration of PCMB or PCMBS to 1 × 10?3m. The enzyme requires phospholipid for activity. Incubation with phospholipase C inhibits activity and subsequent addition of lecithin-containing saturated fatty acids partially restores activity, whereas lecithin-containing unsaturated fatty acids further inhibit activity. |
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