A Microsomal Nucleoside Diphosphatase

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A microsomal nucleoside diphosphatase.

s of the first annual meeting of the American Societyfor Cell Biology, 1961, p. 155. NOVIKOFF, A. B., ESSNER, E., GOLDFISCHER, S., AND HEUS,M., Symposium Intern. Sot. Cell Biol., 1, 149 (1962).NOVIKOFF, A. B., AND GOLDFISCHER, S., Fifth InternationalCongress of Biochemistry,Moscow, 1961, p. 184.NOVIKOFF, A. B., AND GOLDFISCHER. S., Proc. Natl. Acad.hi. U.S., 47, 802 ...

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Nucleotide Metabolism by Microsomal UDP-Glucuronyltransferase and Nucleoside Diphosphatase as Determined by 31P

31p n.m.r. spectroscopy was used to study the nucleotide kinetics of UDP-glucuronyltransferase and associated reactions in the liver microsomal fraction. The effects of Mg2+ and EDTA on these reactions were investigated qualitatively. It was found that the rabbit microsomal fraction has no nucleoside pyrophosphatase activity, that UDP was immediately hydrolysed and that it was released from the...

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Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities.

We have demonstrated that acylphosphatase possesses ATP-diphosphohydrolase (apyrase-like) activity. In fact, acylphosphatase first catalyses the hydrolysis of the gamma-phosphate group of nucleoside triphosphates, and then attacks the beta-phosphate group of the initially produced nucleoside diphosphates, generating nucleoside monophosphates. In contrast, it binds nucleoside monophosphates but ...

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Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence.

We identified SA1684 as a Staphylococcus aureus virulence gene using a silkworm infection model. The SA1684 gene product carried the DUF402 domain, which is found in RNA-binding proteins, and had amino acid sequence similarity with a nucleoside diphosphatase, Streptomyces coelicolor SC4828 protein. The SA1684-deletion mutant exhibited drastically decreased virulence, in which the LD50 against s...

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A steady-state kinetic analysis of nucleoside diphosphatase activity of Golgi membranes.

( i ) Treatment of microsomes with 0.9% (w/v) CHAPS and dilution to 0.3% resulted in an approx. 6-fold increase in specific activity compared with solubilization using 0.3% (w/v) CHAPS only. The native high molecular mass activity, approx. 200 kDa [6] , was maintained after this treatment. ( i i ) Application of solubilized microsomes to DEAE-52 cellulose gave an unbound and a bound peak of act...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1963

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)81323-0