Results 211 to 220 of about 232,598 (258)
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Lactate Dehydrogenase

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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The disproportionation of glyoxylate by lactate dehydrogenase

Archives of Biochemistry and Biophysics, 1980
Abstract 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, 1967
IF 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 and the Diagnosis of Malaria

Parasitology Today, 1998
Over the past five years, several methods have been developed that exploit the differences between Plasmodium lactate dehydrogenase (pLDH) and the human LDH isoforms for the purposes of measuring pLDH in blood and in in vitro cultures. These methods have been incorporated into an easy screening method for the identification and quantitation of parasite
M T, Makler, R C, Piper, W K, Milhous
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Lactate dehydrogenase in rat mitochondria

Archives of Biochemistry and Biophysics, 1987
Small but persistent amounts of L-lactate dehydrogenase (LDH) activity were found in mitochondrial preparations isolated from rat heart, kidney, liver, and lymphocytes. Brain mitochondrial preparations were also isolated, but the results were inconclusive.
R B, Brandt   +3 more
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Immunochemical studies on lactate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973
Abstract 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 ...
J F, Burd, M, Usategui-Gomez
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Lactate Dehydrogenases in Human Testes

Science, 1963
A unique form of lactate dehydrogenase was observed in the starch-gel electrophoretic patterns of adult human testes. It was present in sperm, but absent in prepubertal testes. Its electrophoretic mobility, heat stability, kinetic behavior with pyridine nucleotide analogs, and chromatographic characteristics on diethylaminoethyl cellulose were ...
A, Blanco, W H, Zinkham
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Regulatory characteristics of lactate dehydrogenases

Advances in Enzyme Regulation, 1972
Abstract 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.
N O, Kaplan, J, Everse
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[Lactate dehydrogenase (LDH)].

Nihon rinsho. Japanese journal of clinical medicine, 1995
The quantitative distribution of the lactate dehydrogenase (LDH) isozymes is different and characteristic. Therefore, when the LDH isozymes are released from tissue to serum, as on cell injury, the serum LDH isozyme pattern changes and in a sense resembling the profile of the affected tissue.
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Lactate dehydrogenase and trypanosomes

Transactions of the Royal Society of Tropical Medicine and Hygiene, 1970
W E, Ormerod   +3 more
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