Results 181 to 190 of about 25,315 (221)

Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani

Molecular and Biochemical Parasitology, 2007
Trypanosomatid protozoan pathogens are purine auxotrophs that are highly dependent on the enzyme inosine monophosphate dehydrogenase (IMPDH) for the synthesis of guanylate nucleotides. Enzymatic characterization of the Leishmania donovani IMPDH (LdIMPDH) overexpressed in E.
Fredrick, Dobie, Amanda, Berg, Jan M, Boitz, Armando, Jardim   +3 more
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Concentration of Inosine 5′‐Monophosphate in Meat

Journal of Food Science, 1967
SUMMARY Concentrations of inosine 5′‐monophosphate (IMP) were not significantly different in the longissimus dorsi, biceps femoris, and semimembranosus muscles of six pork carcasses sampled 48 hr post‐mortem. On aging beef for 28 days at 0.1–1.5°C (33–35°F) the peak concentration of IMP (5.4 μM/g) occurred at 12.hr post‐mortem.
R. D. DANNERT, A. M. PEARSON
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Studies on inosine monophosphate dehydrogenase. An associating-dissociating system

Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
The techniques of polyacrylamide gel electrophoresis, sedimentation velocity and frontal analysis on Sephadex have been used to demonstrate that preparations of IMP dehydrogenase (IMP: NAD+ oxidoreductase, EC 1.2.1.14) from Aerobacter aerogenes consist of a mixture of molecular weight isomers.
E, Heyde, J F, Morrison
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Novel amide-based inhibitors of inosine 5′-monophosphate dehydrogenase

Bioorganic & Medicinal Chemistry Letters, 2002
A series of novel amide-based small molecule inhibitors of inosine monophosphate dehydrogenase (IMPDH) was explored. The synthesis and the structure-activity relationships (SARs) derived from in vitro studies are described.
Scott H, Watterson, Chunjian, Liu, T G Murali, Dhar, Henry H, Gu, William J, Pitts, Joel C, Barrish, Catherine A, Fleener, Katherine, Rouleau, N Z, Sherbina, Diane L, Hollenbaugh, Edwin J, Iwanowicz   +10 more
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Rapid synthesis of triazine inhibitors of inosine monophosphate dehydrogenase

Bioorganic & Medicinal Chemistry Letters, 2002
A series of novel triazine-based small molecule inhibitors (IV) of inosine monophosphate dehydrogenase was prepared. The synthesis and the structure-activity relationships (SAR) derived from in vitro studies are described.
William J, Pitts, Junqing, Guo, T G Murali, Dhar, Zhongqi, Shen, Henry H, Gu, Scott H, Watterson, Mark S, Bednarz, Bang Chi, Chen, Joel C, Barrish, Donna, Bassolino, Daniel, Cheney, Catherine A, Fleener, Katherine A, Rouleau, Diane L, Hollenbaugh, Edwin J, Iwanowicz   +14 more
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Direct assay method for inosine 5′-monophosphate dehydrogenase activity

Analytical Biochemistry, 1985
A rapid microassay method for the accurate measurement of the activity of inosine 5'-monophosphate dehydrogenase in crude tissue extracts was described. [8-14C]IMP and the radioactive products were separated by high-voltage electrophoresis in 0.1 M potassium phosphate buffer, pH 7.0, for 45 min.
T, Ikegami, Y, Natsumeda, G, Weber
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The amination of inosine monophosphate in skeletal muscle

Archives of Biochemistry and Biophysics, 1961
Abstract Dialyzed extracts of skeletal muscle are capable of synthesizing adenylosuccinic acid by the condensation of inosine monophosphate and aspartic acid. In undialyzed extracts adenylosuccinic acid once formed is converted to adenine nucleotides.
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Studies on inosine monophosphate dehydrogenase. Isotope exchange at equilibrium

Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
Investigations on the mechanism of the IMP dehydrogenase (IMP: NAD+ oxidoreductase, EC 1.2.1.14) reactions have been made at pH 7.0 by measuring rates of isotope exchange at chemical equilibrium with K+ maintained at a constant concentration. The results are generally in accord with the conclusions reached on the basis of the steady-state kinetic data ...
E, Heyde, J F, Morrison
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Purification and specificity of antibodies to inosine 5'-monophosphate

Biochimie, 1977
Antibodies to inosine 5'-monophosphate elicited in rabbits by immunization with a conjugate of IMP (oxidized with periodate) and bovine serum albumin have been purified by affinity chromatography. By the use of two affinity columns, Sepharose-IMP and Sepharose-oligo(I), the antibodies have been fractionated into three fractions.
E, Sage, M, Leng
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An enzymatic inosine 5′-monophosphate assay of increased specificity

Analytical Biochemistry, 1985
The enzymatic inosine 5'-monophosphate assay described by Grassl [in, Methods of Enzymatic Analysis (H. U. Bergman, ed.), pp. 2168-2171, Academic Press, New York (1974)] is highly nonspecific, as ITP, ATP, ADP, AMP, and adenosine react stoichiometrically.
H T, Kyriazi, R E, Basford
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