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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
openaire   +2 more sources

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
openaire   +3 more sources

Printed paper sensors for serum lactate dehydrogenase using pullulan-based inks to immobilize reagents.

Analytical Chemistry, 2015
In this study, a paper-based point-of-care (POC) colorimetric biosensor was developed for the detection of lactate dehydrogenase in serum using a nonporous, oxygen impermeable reversibly gelling polysaccharide material based on pullulan.
Balamurali Kannan   +5 more
semanticscholar   +1 more source

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
openaire   +3 more sources

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
openaire   +2 more sources

[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.
openaire   +2 more sources

Lactate dehydrogenase and trypanosomes

Transactions of the Royal Society of Tropical Medicine and Hygiene, 1970
S.G. Welch   +3 more
openaire   +3 more sources

Acetylation of lactate dehydrogenase B drives NAFLD progression by impairing lactate clearance.

Journal of Hepatology, 2020
Tongxin Wang   +15 more
semanticscholar   +1 more source

The Turnover Characteristics of Lactate Dehydrogenase

1982
Publisher Summary The combination of the double-isotope approach with the separatory procedures of chromatography and gel electrophoresis is a powerful tool for the determination of relative turnover characteristics. Despite the complications of heterogeneity and compartmentation that bedevil many turnover assessments, this combined approach has ...
openaire   +3 more sources

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