[2] Isocitrate dehydrogenase, malate dehydrogenase, and glutamate dehydrogenase from Archaeoglobus fulgidus

Author(s):  
Ida Helene Steen ◽  
Hilde Hvoslef ◽  
Torleiv Lien ◽  
Nils-Kåre Birkeland
2019 ◽  
Vol 11 (1) ◽  
pp. 116-120
Author(s):  
Mamata Ranot ◽  
Rajesh Sharma

Pinus gerardiana (Chilgoza) is a small to medium sized evergreen tree yielding a highly valuable edible nut. The present investigations were undertaken to assess the different isozymes in Chilgoza pine. Seven isozymes viz., MDH (Malate dehydrogenase), GDH (Glutamate dehydrogenase), SKDH (Shikimic acid dehydrogenase), 6PGDH (6-Phosphogluconate dehydrogenase), MNR (Menadione reductase), IDH (Isocitrate dehydrogenase) and ADH (Alcohol dehdrogenase) were studied. A total of sixteen gene loci were recorded for seven enzyme systems out of which 6 loci namely MDH- A, 6PGDH- A, SKDH- A, IDH- B, MNR- B and ADH- A were polymorphic whereas the remaining ten gene loci i.e. MDH- B, MDH- C, MDH- D, GDH- A, 6PGDH- B, SKDH- B, IDH- A, MNR- A, MNR- B and ADH- B showed no variation. The percentage of polymorphic loci and average number of alleles per locus are one of the useful criterions for comparing species of populations for genetic diversity.


Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt

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.


1974 ◽  
Vol 13 (1-2) ◽  
pp. 79-82
Author(s):  
R.P. Creagan ◽  
B. Carritt ◽  
S. Chen ◽  
R. Kucherlapati ◽  
F.A. McMorris ◽  
...  

1997 ◽  
Vol 250 (2) ◽  
pp. 252-253 ◽  
Author(s):  
Mamoru Wakayama ◽  
Kazue Takashima ◽  
Yuko Tau ◽  
Sadatoshi Nakashima ◽  
Kenji Sakai ◽  
...  

1982 ◽  
Vol 9 (1) ◽  
pp. 47 ◽  
Author(s):  
D Nash ◽  
LG Paleg ◽  
JJ Wiskich

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.


1968 ◽  
Vol 107 (4) ◽  
pp. 455-465 ◽  
Author(s):  
C. Chapman ◽  
W Bartley

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase and NADH–cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP+-linked) and NADPH–cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD+- and NADP+-linked), α-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, α-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD+- and NADP+-linked), glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.


1979 ◽  
Vol 192 (1) ◽  
pp. 33-46 ◽  
Author(s):  
Leonard A. Fahien ◽  
Edward Kmiotek ◽  
Linda Smith

1969 ◽  
Vol 114 (3) ◽  
pp. 455-461 ◽  
Author(s):  
Roxane McKay ◽  
R. Druyan ◽  
G. S. Getz ◽  
M. Rabinowitz

Intramitochondrial loci for δ-aminolaevulate synthetase and ferrochelatase, the initial and final enzymes in haem synthesis, have been found in rat liver. Two different methods of fractionation were applied to mitochondria: (a) sonication and density-gradient centrifugation; (b) treatment with digitonin and differential centrifugation. Similar results were obtained with each technique. δ-Aminolaevulate synthetase is distributed similarly to two known matrix enzymes, malate dehydrogenase and glutamate dehydrogenase. Ferrochelatase is firmly bound to the the inner mitochondrial membrane. These results are considered in terms of the regulation of haem synthesis and in relation to mitochondrial biogenesis.


Sign in / Sign up

Export Citation Format

Share Document