Results 181 to 190 of about 6,159 (212)
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Altered metabolism of the guanosine tetraphosphate, ppGpp, in mutants of E. coli
Cell, 1974Abstract The metabolism of ppGpp is altered in commonly used mutants of E. coli. While retaining their ability to increase rapidly the intracellular level of the nucleotide during amino acid or carbon source deprivation, they are impaired in their ability to reduce an elevated level.
Gudrun Stamminger, Robert A. Lazzarini
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Journal of Biotechnology, 1995
A rapid transient increase of guanosine 3'-diphosphate 5'-diphosphate (ppGpp) in Escherichia coli was found in response to short-term glucose fluctuations that may occur in large-scale fed-batch cultivations. The concentration of ppGpp was measured in laboratory-scale glucose limited fed-batch cultivations.
P, Neubauer +4 more
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A rapid transient increase of guanosine 3'-diphosphate 5'-diphosphate (ppGpp) in Escherichia coli was found in response to short-term glucose fluctuations that may occur in large-scale fed-batch cultivations. The concentration of ppGpp was measured in laboratory-scale glucose limited fed-batch cultivations.
P, Neubauer +4 more
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International Journal of Biochemistry, 1982
1. An enzyme has been partially purified from Ehrlich ascites tumour cells which specifically hydrolyses dinucleosidetetraphosphates, with Km values of around 2 microM. The products of the hydrolysis are the corresponding nucleoside tri- and monophosphates. Dinucleoside Tri- and diphosphates were not substrates of the reaction. 2.
A, Moreno +3 more
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1. An enzyme has been partially purified from Ehrlich ascites tumour cells which specifically hydrolyses dinucleosidetetraphosphates, with Km values of around 2 microM. The products of the hydrolysis are the corresponding nucleoside tri- and monophosphates. Dinucleoside Tri- and diphosphates were not substrates of the reaction. 2.
A, Moreno +3 more
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Biochimica et Biophysica Acta (BBA) - General Subjects, 1978
Guanosine 5'-tetraphosphate (GTP4) stimulated mammalian adenylate cyclase activity at concentrations down to 1 micronM. Greater stimulatory activity was apparent with lung than with heart, brain or liver from the rat. At a concentration of 0.1 mM, GTP4 stimulated lung adenylate cyclase activity from rat, guinea pig and mouse about four-fold.
L J, Ignarro, R A, Gross
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Guanosine 5'-tetraphosphate (GTP4) stimulated mammalian adenylate cyclase activity at concentrations down to 1 micronM. Greater stimulatory activity was apparent with lung than with heart, brain or liver from the rat. At a concentration of 0.1 mM, GTP4 stimulated lung adenylate cyclase activity from rat, guinea pig and mouse about four-fold.
L J, Ignarro, R A, Gross
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Ribonucleoside 3'-di- and -triphosphates. Synthesis of guanosne tetraphosphate (ppGpp)
Biochemistry, 1975A procedure has been outlined for the synthesis of ribonucleoside 3'-di- and -triphosphates. The synthetic scheme involves the conversion of a ribonucleoside 3'-monophosphate to its 2'-(5'-di)-O-(1-methoxyethyl) derivative, followed by successive treatments of the blocked ribonucleotide with 1,1'-carbonyldiimidazole and mono(tri-n-butylammonium ...
J W, Kozarich, A C, Chinault, S M, Hecht
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Journal of cyclic nucleotide research, 1977
The effects of a variety of purine and pyrimidine nucleotides were tested for their capacity to inhibit mammalian soluble guanylate cyclase activity. Adenosine 5'-tetraphosphate (ATetP), ATP, ADP, AMP, guanosine 5'-tetraphosphate (GTetP) and GDP were found to inhibit soluble guanylate cyclase activity from rat lung and other mammalian tissues.
L J, Ignarro, R A, Gross, D M, Gross
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The effects of a variety of purine and pyrimidine nucleotides were tested for their capacity to inhibit mammalian soluble guanylate cyclase activity. Adenosine 5'-tetraphosphate (ATetP), ATP, ADP, AMP, guanosine 5'-tetraphosphate (GTetP) and GDP were found to inhibit soluble guanylate cyclase activity from rat lung and other mammalian tissues.
L J, Ignarro, R A, Gross, D M, Gross
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Biochemistry. Biokhimiia, 1998
A cytosolic preparation of Saccharomyces cerevisiae is capable of hydrolyzing adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate with activities which are 1.5-2 times greater than that with polyP15. The apparent K(m) values for hydrolysis of adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate are 100 and 80 microM, respectively.
T V, Kulakovskaya +2 more
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A cytosolic preparation of Saccharomyces cerevisiae is capable of hydrolyzing adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate with activities which are 1.5-2 times greater than that with polyP15. The apparent K(m) values for hydrolysis of adenosine-5'-tetraphosphate and guanosine-5'-tetraphosphate are 100 and 80 microM, respectively.
T V, Kulakovskaya +2 more
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Trimethoprim-induced accumulation of guanosine tetraphosphate (ppGpp) in
Biochemical and Biophysical Research Communications, 1972S.R. Khan, Hiroshi Yamazaki
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