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C Lowery

Publications and source records attributed to C Lowery.

8 recordsLinked to original sources
PubMed1979

Triglyceride lipase activity and human platelets.

The activity of triglyceride lipases in human postheparin plasma is significantly higher in platelet rich than platelet poor plasma. This holds for total activity, lipoprotein lipase (LPL) activity, and hepatic triglyceride lipase (H-TGL) activity. Gel filtration of platelet rich postheparin plasma on Sepharose 2 B will separate platelets from triglyceride lipase activity. The very small triglyceride lipase activity of isolated platelets is inhibited by 1.0 M NaCl, slightly inhibited by specific antibody to hepatic lipase, and not influenced by specific antibody to lipoprotein lipase.

Blood Platelets↗
PubMed1977

Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesi termination factor p. I. Enzymatic properties and effects of inhibitors.

The purification of p protein to homogeneity from Escherichia coli has shown that its RNA-dependent ATPase activity is physically inseparable from its termination activity. The biochemical properties of pATPase have been studied using poly(C) as the activating RNA. This reaction is stimulated by Mg2+ ions and Mn2+ ions and is prevented by excess EDTA; it is not stimulated by Ca2+ ions. The reaction is not affected by a Zn2+ ion chelator and is inhibited by 1 mM Zn2+. With Mg2+ present, the activity is essentially constant from pH 7 to pH 9.7. pATPase is sensitive to p-hydroxymercuribenzoate and to N-ethylmaleimide. All four ribonucleoside triphosphates are hydrolyzed by p action. ATP has the lowest Km (0.009 mM), while CTP has the highest Vmax. In a mixture containing all four nucleoside triphosphates at a concentration of 0.4 mM, p shows no strong preference for any one of the substrates. The response of p ATPase to a variety of inhibitors of other ATPases and GTPases and of transcription has been studied. Of the compounds tested, aurintricarboxylic acid, an inhibitor of protein-nucleic acid interactions, was found to be a potent inhibitor of p ATPase, while rifampicin and heparin had no effect. pATPase showed partial sensitivity to thiostrepton, fusidic acid, Dio 9, and sodium azide.

Adenosine Triphosphatases↗
PubMed1977

Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor p. II. Influence of synthetic RNA homopolymers and random copolymers on the reaction.

The ability of various kinds of RNA molecules to activate the ATP hydrolysis reaction catalyzed by the p transcription termination factor from Escherichia coli has been studied. The most active RNA polymers are those containing cytidylate residues and very little ordered structure. Free poly(C) is the most active homopolymer; it is 45 times more active than poly(U), which is the only non-cytidine containing RNA that has detectable activity. Poly(C) has no activity when complexed with poly(I) or when the chain lengths are shorter than 22 nucleotides long. Although cytidylate residues are important they need not be frequent; a random copolymer of uridine and cytidine nucleotides with as few as 1 cytidylate residue out of 20 is as active as poly(C). The extent of activation with poly(C) depends on the ratio of p to poly(C). Poly(C) becomes saturated with p at a ratio of 1.8 ng of p/pmol poly(C), which is equivalent to one p monomer/27 nucleotides. A further increase in this ratio leads to a reduction in p activity. Decreasing the length of the poly(C) does not alter the observed saturation value but does decrease the rate of ATP hydrolysis when the RNA is in excess. The possible relevance of these results to p termination activity is discussed.

Adenosine Triphosphatases↗
PubMed1975

Transcription termination factor rho activity is altered in Escherichia coli with suA gene mutations.

Rho factor has been purified from a strain of E. coli containing the Su78 mutation in the suA gene and assayed in another strain with an amber mutation in the suA gene. The rho from the Su78 mutant strain is present in normal amounts but has altered termination function; it does not terminate transcription at some sites that are recognized effectively by the rho factor from the isogenic wild-type strain. Rho in cells with an amber mutation in the suA gene has been assayed by its RNA-dependent ATPase activity. Extracts of cells of this strain have only 9% as much of this rho activity as extracts of cells of the isogenic wild-type strain. These results suggest that rho is the product of the suA gene. Since mutations in the suA gene are known to decrease polar effects of mutations in other genes, it is also suggested that rho factor is at least partially responsible for polar effects.

Bacterial Proteins↗