Individual variation of nucleoside triphosphate pyrophosphohydrolase activity in human erythrocytes, granulocytes, lymphocytes, and platelets

1980 ◽  
Vol 18 (3-4) ◽  
pp. 235-245 ◽  
Author(s):  
Vernon L. Verhoef ◽  
Steven A. Fuller ◽  
Allan J. Morris
Keyword(s):  
Individual Variation ◽  
Human Erythrocytes ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Pyrophosphohydrolase

Relationships between nucleoside triphosphate pyrophosphohydrolase activity and inosine triphosphate accumulation in human erythrocytes

1976 ◽  
Vol 54 (10) ◽  
pp. 843-847 ◽  
Author(s):  
Christian Sober ◽  
J. Frank Henderson ◽  
George Zombor ◽  
Ernest E. McCoy ◽  
Vernon Verhoef ◽  
...  
Keyword(s):  
Specific Activity ◽  
Human Erythrocytes ◽  
Nucleoside Triphosphate ◽  
Human Red Blood Cells ◽  
Nucleoside Triphosphate Pyrophosphohydrolase ◽  
Specific Activities ◽  
Two Parameters ◽  
Relationship Of ◽  
The Relationship

The relationship between nucleoside triphosphate pyrophosphohydrolase (NTPH) (EC 3.6.1.19) activity in erythrocyte lysates and accumulation of radioactive inosine triphosphate (ITP) in human erythrocytes incubated in vitro with [14C]hypoxanthine, was studied in 93 humans. When ITP accumulation, expressed as percentage of total radioactive nucleotides, was plotted against NTPH specific activity, an inverse relationship was found to exist. A continuous spectrum of NTPH specific activities and ITP accumulation values exists in the human population and the relationship between these two parameters follows the relationship of substrate concentration to enzyme activity predicted by Michaelis–Menten enzyme kinetics. One interpretation of these data is that the ITP concentration in human red blood cells is controlled by the degradation of ITP to IMP and pyrophosphate catalyzed by NTPH.

Solution Structure of the MutT Enzyme, a Nucleoside Triphosphate Pyrophosphohydrolase

Biochemistry ◽  
1995 ◽  
Vol 34 (46) ◽  
pp. 14997-15005 ◽  
Author(s):  
Chitrananda Abeygunawardana ◽  
David J. Weber ◽  
Apostolos G. Gittis ◽  
David N. Frick ◽  
Jian Lin ◽  
...  
Keyword(s):  
Solution Structure ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Pyrophosphohydrolase

scholarly journals MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase in Escherichia coli

2002 ◽  
Vol 184 (19) ◽  
pp. 5323-5329 ◽  
Author(s):  
Junjie Zhang ◽  
Masayori Inouye
Keyword(s):  
Escherichia Coli ◽  
Direct Interaction ◽  
Kanamycin Resistance ◽  
Nucleoside Triphosphate ◽  
Cellular Functions ◽  
Genomic Libraries ◽  
E Coli ◽  
Yeast Two Hybrid System ◽  
Nucleoside Triphosphate Pyrophosphohydrolase

ABSTRACT Era is an essential GTPase in Escherichia coli, and Era has been implicated in a number of cellular functions. Homologues of Era have been identified in various bacteria and some eukaryotes. Using the era gene as bait in the yeast two-hybrid system to screen E. coli genomic libraries, we discovered that Era interacts with MazG, a protein of unknown function which is highly conserved among bacteria. The direct interaction between Era and MazG was also confirmed in vitro, being stronger in the presence of GDP than in the presence of GTPγS. MazG was characterized as a nucleoside triphosphate pyrophosphohydrolase which can hydrolyze all eight of the canonical ribo- and deoxynucleoside triphosphates to their respective monophosphates and PPi, with a preference for deoxynucleotides. A mazG deletion strain of E. coli was constructed by replacing the mazG gene with a kanamycin resistance gene. Unlike mutT, a gene for another conserved nucleotide triphosphate pyrophosphohydrolase that functions as a mutator gene, the mazG deletion did not result in a mutator phenotype in E. coli.

Individual variation in inosine triphosphate accumulation in human erythrocytes

1975 ◽  
Vol 8 (1-6) ◽  
pp. 353-364 ◽  
Author(s):  
Joyce H. Fraser ◽  
Helene Meyers ◽  
J. Frank Henderson ◽  
Larry W. Brox ◽  
Ernest E. McCoy
Keyword(s):  
Individual Variation ◽  
Human Erythrocytes
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