Results 361 to 370 of about 785,757 (422)

Lactate Dehydrogenase in Tears

American Journal of Ophthalmology, 1980
Lactate dehydrogenase levels in tears were measured in normal subjects and in patients with retinoblastoma. When specimens were collected without trauma in normal subjects, there were usually no detectable levels of lactate dehydrogenase. When the eyelids were rubbed (probably liberating epithelial cells) lactate dehydrogenase levels were detectable ...
Cynthia J. MacKay, Robert M. Ellsworth, Michael Pesche, F. David Kitchin, David H. Abramson   +4 more
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Lactate dehydrogenases in cyanobacteria

Archives of Microbiology, 1975
NAD-linked lactate dehydrogenases specific for the D- and L-lactate have been demonstrated in a number of strains of unicellular cyanobacteria. The D-lactate dehydrogenase of one strain (Synechococcus 6716) was partially purified and its properties were studied. The enzyme has a molecular weight of ca.
Michael Doudoroff, J. J. Sanchez, N. J. Palleroni, Joan Duong   +3 more
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Analysis of Cell Viability by the Lactate Dehydrogenase Assay.

Cold Spring Harbor Protocols, 2018
A common method for determining cytotoxicity is based on measuring the activity of cytoplasmic enzymes released by damaged cells. Lactate dehydrogenase (LDH) is a stable cytoplasmic enzyme that is found in all cells. LDH is rapidly released into the cell
Priti Kumar, Arvindhan G. Nagarajan, P. Uchil   +2 more
semanticscholar   +1 more source

The Biochemical and Clinical Perspectives of Lactate Dehydrogenase: An Enzyme of Active Metabolism.

Endocrine, Metabolic & Immune Disorders - Drug Targets, 2019
BACKGROUND Lactate dehydrogenase (LDH) is a group of oxidoreductase isoenzymes catalyzing the reversible reaction between pyruvate and lactate. The five isoforms of this enzyme, formed from two subunits vary in isoelectric points and these isoforms have ...
A. Khan, Khaled S. Allemailem, F. Alhumaydhi, S. Gowder, A. Rahmani   +4 more
semanticscholar   +1 more source

Lactate dehydrogenase isoenzymes

Journal of Chromatography B: Biomedical Sciences and Applications, 1988
The analytical procedures for LD isoenzymes include electrophoresis, chromatography, immunochemical and kinetic methods. Electrophoretic methods are generally preferred because the resulting patterns are directly observable and all five isoenzymes are resolved in a single procedure.
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Lactate Dehydrogenases in Human Testes [PDF]

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 ...
Antonio Blanco, William H. Zinkham
openaire   +2 more sources

Elevated lactate dehydrogenase (LDH) can be a marker of immune suppression in cancer: Interplay between hematologic and solid neoplastic clones and their microenvironments.

Cancer Biomarkers, 2017
Metabolism of neoplastic cells is shifted toward high glucose uptake and enhanced lactate production. Lactate dehydrogenase (LDH), which is comprised of two major subunits, LDH-A and LDH-B, reversibly catalyzes the conversion of pyruvate to lactate or ...
Jennifer Ding, J. Karp, A. Emadi
semanticscholar   +1 more source

Lactate Dehydrogenases in Oomycetes

Mycologia, 1972
Lactate dehydrogenases [D(-)-lactate: NAD oxidoreductase, E.C. 1.1.1.28] have recently been detected in a number of lower fungi particularly among the Oomycetes (Gleason and Price, 1969; Warren and Mullins, 1969; LeJohn, 1971) and the Chytridiomycetes (Gleason and Price, 1969; LeJohn, 1971).
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Lactate Dehydrogenase Isoenzymes [PDF]

, 1970
The heterogeneity of lactate dehydrogenase was first recognized when Neilands (1952) demonstrated activity in each of the two electrophoretically distinct proteins, previously separated by Meister (1950) from the crystalline ox-heart enzyme. Subsequently Vesell and Bearn (1957) found three distinct components when human sera were subjected to starch ...
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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.
Edward S. Kline, Richard B. Brandt, Jerome E. Laux, Stephen E. Spainhour   +3 more
openaire   +2 more sources