Confirmation of the Synteny of the Human Genes for Cytoplasmic Isocitrate Dehydrogenase and Cytoplasmic Malate Dehydrogenase and Assignment to Chromosome 2

1974 ◽  
Vol 13 (1-2) ◽  
pp. 79-82
Author(s):  
R.P. Creagan ◽  
B. Carritt ◽  
S. Chen ◽  
R. Kucherlapati ◽  
F.A. McMorris ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Chromosome 2 ◽  
Human Genes

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

Effect of Proline, Betaine and Some Other Solutes on the Heat Stability of Mitochondrial Enzymes

1982 ◽  
Vol 9 (1) ◽  
pp. 47 ◽  
Author(s):  
D Nash ◽  
LG Paleg ◽  
JJ Wiskich
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Plant Mitochondria ◽  
Heat Stability ◽  
Heat Inactivation ◽  
Mitochondrial Enzymes

When isolated plant mitochondria are heated, isocitrate dehydrogenase, malate dehydrogenase and fumarase lose activity at different rates. The rate of loss of activity of each enzyme is reduced if the mitochondria are heated in the presence of proline, betaine or some other solutes; protection by proline or betaine against heat inactivation is also evident with these enzymes when they are solubilized. NAD-isocitrate dehydrogenase in pea mitochondria and NADP-dependent isocitrate dehydrogenase of pea chloroplasts are also protected by proline and betaine against inactivation when the isolated organelles are heated.

Radiation Hybrid Mapping of Human Cytosolic Malate Dehydrogenase (hcMDH) to the Short Arm of Chromosome 2

1999 ◽  
Vol 25 (2) ◽  
pp. 109-113 ◽  
Author(s):  
Agnes Shuk Yee Lo ◽  
Choong Tsek Liew ◽  
Patrick Tik Wan Law ◽  
Mercè Garcia-Barceló ◽  
Stephen Kwok Wing Tsui ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Radiation Hybrid ◽  
Radiation Hybrid Mapping ◽  
Chromosome 2 ◽  
Hybrid Mapping ◽  
Cytosolic Malate Dehydrogenase

Effects of Various Solutes on the Thermostability of Isocitrate Dehydrogenase and Malate Dehydrogenase of Isolated Plant Mitochondria.

1982 ◽  
Vol 9 (6) ◽  
pp. 715 ◽  
Author(s):  
D Nash ◽  
JT Wiskich
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Choline Chloride ◽  
Plant Mitochondria ◽  
Membrane Integrity ◽  
Triticum Aestivum L ◽  
Osmotic Effect ◽  
Pisum Sativum L ◽  
Wheat Leaves ◽  
Brassica Oleracea L

Proline and betaine increased the thermostability of NAD-isocitrate dehydrogenase (EC 1.1.1.41) and of NAD-malate dehydrogenase (EC 1.1.1.37) when mitochondria isolated from pea leaves (Pisum sativum L.), wheat leaves (Triticum aestivum L.) and cauliflower buds (Brassica oleracea L.) were heated. Potassium chloride and choline chloride also increased the thermostability of isocitrate dehydrogenase in the three species, but their effects on malate dehydrogenase varied. Protection was found with both intact and disrupted mitochondria, indicating that it was not dependent on an osmotic effect. Proline and KCl also prolonged membrane integrity, as measured by impermeability to NAD+, during heating of pea leaf and cauliflower bud mitochondria. Phenylalanine reduced the thermostability of isocitrate dehydrogenase, indicating that protection is not a general solute effect.

scholarly journals Enzymic changes in rabbit and rat mammary gland during the lactation cycle

1969 ◽  
Vol 112 (3) ◽  
pp. 293-301 ◽  
Author(s):  
Bilquis Gul ◽  
R. Dils
Keyword(s):  
Mammary Gland ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Pyruvate Carboxylase ◽  
Acid Synthesis ◽  
Mitochondrial Fraction ◽  
Soluble Form ◽  
Supernatant Fraction ◽  
Rat Mammary Gland ◽  
Lactation Cycle

1. Activities of glucose 6-phosphate dehydrogenase (EC 1.1.1.49), 6-phosphogluconate dehydrogenase (EC 1.1.1.44), isocitrate dehydrogenase (EC 1.1.1.42), malate dehydrogenase (EC 1.1.1.37), malate dehydrogenase (decarboxylating) (EC 1.1.1.40), and pyruvate carboxylase (EC 6.4.1.1) were determined in subcellular fractions of mammary gland from rabbits during pregnancy, at different stages of lactation and during weaning. The results were compared with those obtained in similar experiments with rat mammary gland. 2. Three bases of expression of the activity of enzymes in the particle-free supernatant fraction of mammary gland were compared. During lactation, activity expressed per mg. of particle-free supernatant protein (uncorrected for milk protein) correlated well with that expressed per μg. of DNA phosphorus. The disadvantages of expressing activities per g. wet wt. are discussed. 3. The major differences between the two tissues were: (a) neither malate dehydrogenase (decarboxylating) nor a soluble form of pyruvate carboxylase could be detected in rabbit mammary gland at any stage of the lactation cycle; (b) isocitrate dehydrogenase increased in activity during lactation in rabbit mammary gland, but not in that of the rat. 4. Pyruvate carboxylase in the mitochondrial fraction of rabbit mammary gland, and in both the mitochondrial and the soluble fractions of rat mammary gland, did not change in activity during lactation. 5. For each tissue, the NADP-dependent dehydrogenases studied had a high activity at all stages of the lactation cycle compared with the rate of fatty acid synthesis at mid-lactation. The significance of these results is discussed with respect to the supply of NADPH via NADH.

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