Literature DB >> 6291940

An RNA-dependent nucleoside triphosphate hydrolase from Krebs-II ascites tumor cells. Detection and preliminary characterization.

K M Chumakov, M N Rozanov, V I Agol.   

Abstract

A novel enzymatic activity, RNA-dependent, NTPase, was isolated from Krebs-II ascites tumor cells. This activity is associated with ribosomes and can be detached from them by washing in KCl solutions of a higher than 0.3 M concentration. The enzyme hydrolyzes all the four nucleoside triphosphates to the corresponding nucleoside diphosphates and orthophosphate. The rate of NTP hydrolysis increases about 10-fold in the presence of natural RNAs and synthetic polyribonucleotides [except poly(G)]. Natural DNAs, both double and single-stranded, are poor cofactors, although pol(dA) and poly(dT) stimulate, to a certain extent, the rate of ATP hydrolysis. Possible involvement of RNA-dependent NTPase in protein biosynthesis is discussed.

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Year:  1982        PMID: 6291940     DOI: 10.1111/j.1432-1033.1982.tb06871.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Characterization of a ribonuclease-sensitive nucleoside triphosphatase activity from HeLa nuclei.

Authors:  L V Richardson; J P Richardson
Journal:  Biochem J       Date:  1985-04-15       Impact factor: 3.857

2.  Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.

Authors:  P Blount; S I Sukharev; P C Moe; M J Schroeder; H R Guy; C Kung
Journal:  EMBO J       Date:  1996-09-16       Impact factor: 11.598

3.  Rod outer segment structure influences the apparent kinetic parameters of cyclic GMP phosphodiesterase.

Authors:  C L Dumke; V Y Arshavsky; P D Calvert; M D Bownds; E N Pugh
Journal:  J Gen Physiol       Date:  1994-06       Impact factor: 4.086

  3 in total

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