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Lactate Dehydrogenases in Human Testes [PDF]

open access: possibleScience, 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 ...
Antonio Blanco, William H. Zinkham
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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 ...
M. Usategui-Gomez, J.F. Burd
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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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Lactate Dehydrogenase Isozyme and Hypothyroidism

Archives of Internal Medicine, 1985
To 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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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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4 Lactate Dehydrogenase

1975
Publisher Summary This chapter discusses the lactate dehydrogenase. Lactic acid is the end product of anaerobic glycolysis in muscle tissue has been known for all of this century. Cell-free extracts able to catalyze the oxidation of lactate to pyruvate.
Anders Liljas   +3 more
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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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Mitochondrial Lactate Dehydrogenase

1988
The classical lactate dehydrogenase (LDH) catalyzes the interconversion of lactate and pyruvate: $$ Pyruvate + NADH + {H^ + } \leftrightarrow L - lactate + NA{D^ + }\quad $$ The enzyme is present in cytosol of animal tissues and it catalyzes the final reaction of glycolysis.
Jerome E. Laux   +3 more
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Maleimideinactivation of lactate dehydrogenase isozymes

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract The homologous beef lactate dehydrogenase (EC 1.1.1.27) isozymes H 4 and M 4 were observed to be effectively inactivated by a homologous series of N- alkylmaleimides . With each isozyme, the second-order rate constants of inactivation increased with increasing chain length of the alkyl group of the maleimide derivative.
Sharon V. Vercellotti   +2 more
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Pulse Radiolysis of Lactate Dehydrogenase

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1977
Pulse radiolysis has been used to investigate the rates and transient spectra for the reactions of free radicals with beef heart lactate dehydrogenase at pH 7. Analysis of the results leads to second-order rate-constants for eaq-, .OH, .I, .Br2-, .I2- and .(CNS)2- which are, respectively, 24, 21, 10, 0.55, 0.43 and 0.15 in units of 10(10) M-1 s-1 with ...
John D. Buchanan   +3 more
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