Results 161 to 170 of about 223,991 (196)
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Lactate Dehydrogenase in Tears
American Journal of Ophthalmology, 1980Lactate 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 +4 more
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Lactate dehydrogenases in cyanobacteria
Archives of Microbiology, 1975NAD-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 +3 more
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Lactate dehydrogenase isoenzymes
Journal of Chromatography B: Biomedical Sciences and Applications, 1988The 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 Oomycetes
Mycologia, 1972Lactate 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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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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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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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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Lactate dehydrogenase in rat mitochondria
Archives of Biochemistry and Biophysics, 1987Small 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 +3 more
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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
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