Results 301 to 310 of about 344,963 (356)
Some of the next articles are maybe not open access.
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
openaire +3 more sources
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
openaire +3 more sources
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.
openaire +3 more sources
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).
openaire +3 more sources
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
openaire +3 more sources
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 ...
openaire +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
Mortality Prediction with Lactate and Lactate Dehydrogenase
2015It has been proved in many studies that Lactate and Lactate dehydrogenase (LDH) are associated with mortality. In this study lactate test values of inpatients were analyzed with Support Vector Machines (SVM) to identify patients in high risk of death.
Yasemin Zeynep Engin +3 more
openaire +2 more sources