Results 281 to 290 of about 369,761 (340)

Evaluation of Human Cerebrospinal Fluid Malate Dehydrogenase 1 as a Marker in Genetic Prion Disease Patients. [PDF]

open access: yesBiomolecules, 2019
Zerr I   +12 more
europepmc   +1 more source

Pyropheophytin a accompanies pheophytin a in darkened light grown cells of Euglena [PDF]

open access: yes, 1981
Rüdiger, W.   +4 more
core  

The fructose-2,6-bis phosphate system in C-4 plants [PDF]

open access: yes, 1984
Buchanan, Bob B.   +3 more
core  

Evolution of Malate Dehydrogenase in Birds [PDF]

open access: possibleScience, 1966
Heart extracts from over 100 species of birds were subjected to starch-gel electrophoresis at p H 7. The "supernatant" form of malate dehydrogenase, an enzyme present in every extract, was then located on the gels by a specific staining method.
Allan C. Wilson, G. B. Kitto
openaire   +2 more sources
Some of the next articles are maybe not open access.

Related searches:

Stability of dehydrogenases III. malate dehydrogenases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
Cytoplasmic and mitochondrial malate dehydrogenases from pig and chicken were studied by chemical modification of amino groups, hybridization of immobilization. Determination of thermal stability was used to characterize the different species. Modification of amino groups was found to decrease thermal stability especially when neutralization of the ...
Joachim Müller, C. Klein
openaire   +3 more sources

Glutamate dehydrogenase-malate dehydrogenase complex

Archives of Biochemistry and Biophysics, 1979
Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
Linda Lou Smith   +2 more
openaire   +3 more sources

Heterogeneity of supernatant malate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1968
Abstract A way was found to demonstrate electrophoretically that the supernatant portion of pig heart malate dehydrogenase ( l -malate:NAD oxidoreductase, EC 1.1.1.37) is heterogeneous. Other pig organs displayed the same pattern of supernatant malate dehydrogenase forms.
R.J. Kulick, F.W. Barnes
openaire   +3 more sources

Home - About - Disclaimer - Privacy