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Regulatory characteristics of lactate dehydrogenases
Advances in Enzyme Regulation, 1972Abstract In summary, a consideration of the properties of the various LDHs certainly indicates unique regulatory properties which are particularly suitable for the tissues and the animal in which the various LDHs are found.
Nathan O. Kaplan, Johannes Everse
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Immobilized Lactate Dehydrogenases
Israel Journal of Chemistry, 1974AbstractWe have covalently attached pure chicken H4 and M4 lactate dehydrogenase to porous glass beads by a variety of chemical methods. The attachment of these isoenzymes by the glutaraldehyde and diazo linkages generates immobilized enzymes that are stable for months, show decreased substrate (pyruvate) inhibition and exhibit a pH‐rate profile ...
Francis E. Stolzenbach +3 more
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Journal of Medicinal Chemistry, 2016
Human lactate dehydrogenase (hLDH5), a glycolytic enzyme responsible for the conversion of pyruvate to lactate coupled with oxidation of NADH to NAD(+), plays a crucial role in the promotion of glycolysis in invasive tumor cells. Recently, hLDH5 has been
R. Rani, Vinit Kumar
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Human lactate dehydrogenase (hLDH5), a glycolytic enzyme responsible for the conversion of pyruvate to lactate coupled with oxidation of NADH to NAD(+), plays a crucial role in the promotion of glycolysis in invasive tumor cells. Recently, hLDH5 has been
R. Rani, Vinit Kumar
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Mortality Prediction with Lactate and Lactate Dehydrogenase
2015It has been proved in many studies that Lactate and Lactate dehydrogenase (LDH) are associated with mortality. In this study lactate test values of inpatients were analyzed with Support Vector Machines (SVM) to identify patients in high risk of death.
Yasemin Zeynep Engin +3 more
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The disproportionation of glyoxylate by lactate dehydrogenase
Archives of Biochemistry and Biophysics, 1980Abstract Lactate dehydrogenase (EC 1.1.1.27) catalyzes the NAD-dependent oxidation to (oxalate) and reduction (to glycollate) of glyoxylate. The kinetics of this disproportionation are in accord with the usual reaction pathway of lactate dehydrogenase:substrate inhibition with appropriate pH dependence occurs; a steady state in the ratio of NADH to ...
R. Julian, S. Duncan
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Glyoxylate as a Substrate for Lactate Dehydrogenase
Nature, 1967IF 2-oxobutyrate is substituted for pyruvate as substrate for lactate dehydrogenase (LD), it is found to be more readily reduced by the electrophoretically faster moving LD isoenzymes than by the slower moving LD isoenzymes1,2. Because glyoxylate may also serve as a substrate for LD (ref. 3), we investigated the effect of LD isoenzyme fractions on this
M. R. Banner, S. B. Rosalki
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Lactate Dehydrogenase (LDH) as Prognostic Marker in Acute Leukemia Quantitative Method
, 2017Lactate dehydrogenase enzyme was found in animal and human and play important role in gluconeogenesis process. It distributed in all organs, but the mainly distributed in liver.
W. Elbossaty
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2016
Abstract Glucose is transported into neurons and is used as an energy source. It is also transported into astrocytes and is converted to lactate, which is then released to neurons and is used as another energy source. The latter is called the astrocyte–neuron lactate shuttle.
Nagisa Sada, Tsuyoshi Inoue
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Abstract Glucose is transported into neurons and is used as an energy source. It is also transported into astrocytes and is converted to lactate, which is then released to neurons and is used as another energy source. The latter is called the astrocyte–neuron lactate shuttle.
Nagisa Sada, Tsuyoshi Inoue
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Immunochemical studies on lactate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Abstract 1. 1. A purification procedure for the isolation of lactate dehydrogenase isoenzymes ( l -(+)-lactate: NAD + oxidoreductase, EC 1.1.1.27) from human and related sources is described. The following lactate dehydrogenase isoenzymes were prepared: (a) H 4 from human erythrocytes, (b) M 4 from human liver, and (c) M 4 from rhesus monkey ...
M. Usategui-Gomez, J.F. Burd
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Lactate Dehydrogenase Isozyme and Hypothyroidism
Archives of Internal Medicine, 1985To the Editor. —We read with interest the article by Klein and Levey, 1 the letter by Strasberg, 2 and the reply by Klein and Levey. 3 Dr Strasberg pointed out that an elevated lactate dehydrogenase isozyme 1 (LDH , ) level originated from cardiac muscle and "that hypothyroidism should be added to the list of etiologies associated with elevated levels
Junichi Tajiri +3 more
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