ChemInform Abstract: Synthesis and Properties of Some New Platinum Blues Derived from the Reaction of Cis-[Pt(NH3)2(OH2)2]2+ with Pyrimidines and Adenine, and their Inhibition of Two Mitochondrial Enzymes (L-Malate Dehydrogenase and Fumarase) and DNA Synt

1983 ◽  
Vol 14 (23) ◽  
Author(s):  
A. A. ZAKI ◽  
C. A. MCAULIFFE ◽  
M. W. FRIEDMAN ◽  
W. E. HILL ◽  
H. H. KOHL
Keyword(s):  
Malate Dehydrogenase ◽  
Mitochondrial Enzymes

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.

EFFECT OF PREGNANCY ON CYTOPLASMIC AND MITOCHONDRIAL ENZYMES IN HUMAN AND ANIMAL MYOMETRIUM

1974 ◽  
Vol 77 (2) ◽  
pp. 368-379 ◽  
Author(s):  
Helmut Geyer ◽  
Michael Riebschläger
Keyword(s):  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Malate Dehydrogenase ◽  
Human Tissue ◽  
Human Myometrium ◽  
Mitochondrial Enzymes ◽  
Cellular Compartment ◽  
Cellular Localisation ◽  
Specific Activities ◽  
Mitochondrial Malate Dehydrogenase

ABSTRACT An investigation was made on the influence of pregnancy on the specific activities of cytoplasmic (lactate dehydrogenase2), cytoplasmic malate dehydrogenase) and mitochondrial enzymes (glutamate dehydrogenase, mitochondrial malate dehydrogenase, cytochrome-c-oxidase) in the human and animal myometrium. The activities were related to DNA. The specific activities of all the investigated enzymes increased. This rise in activity depended on the cellular localisation of the enzyme. The activity of all enzymes in one cellular compartment changed to the same extent. This change varied according to species. With regard to the human tissue, the increase of the cytoplasmic enzymes was larger than that of the mitochondrial enzymes. In the rat, however, a significantly larger increase of the mitochondrial enzymes was found. The increase in the specific activities of the cytoplasmic enzymes in the human and rat was proportional to the protein-content and to the hypertrophy of the cells. It was concluded that the number of mitochondria or their enzymatic activity increased in both species during pregnancy – in each species, however, to a different extent. The pattern of the LDH-isoenzymes in the myometrium changed in the same manner in the human myometrium as in the rat. The percentage of M subunits of LDH compared to H subunits rose in both cases during pregnancy.

scholarly journals Glucose-induced inactivation of mitochondrial enzymes in the yeast Saccharomyces cerevisiae

1981 ◽  
Vol 198 (2) ◽  
pp. 281-287 ◽  
Author(s):  
M Takeda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Malate Dehydrogenase ◽  
Mitochondrial Enzymes ◽  
Yeast Saccharomyces Cerevisiae ◽  
Cytoplasmic Proteins ◽  
Fructose 1,6 Bisphosphatase ◽  
Specific Activities

1. Addition of glucose induced an inactivation of mitochondrial enzymes in the yeast Saccharomyces cerevisiae containing normal mitochondrial particles. 2. The glucose-induced inactivation of mitochondrial enzymes was inhibited by the presence of cycloheximide. 3. Pepstatin also inhibited the inactivation, but phenylmethanesulphonyl fluoride accelerated the inactivation. 4. The specific activities of fructose 1,6-bisphosphatase and cytoplasmic malate dehydrogenase were decreased on the exposure to glucose, as well as those of the mitochondrial enzymes. However, the glucose-induced inactivation of cytoplasmic enzymes was not inhibited by the presence of pepstatin. 5. The specific activities of hexokinase and phosphofructokinase, which are cytoplasmic enzymes were increased by the addition of glucose, and this effect was not affected by pepstatin. 6. Addition of glucose resulted in an increase in the synthesis of proteins of the mitochondria and the cytosol, and simultaneously in degradation of these mitochondrial and cytoplasmic proteins.

Increased Activity of Some Enzymes in Serum in Cases of Severely Decompensated Diabetes, with and without Ketoacidosis

1972 ◽  
Vol 18 (11) ◽  
pp. 1403-1406 ◽  
Author(s):  
Francesco Belfiore ◽  
Elena Napoli ◽  
Luigi Lo Vecchio
Keyword(s):  
Creatine Kinase ◽  
Malate Dehydrogenase ◽  
Tissue Damage ◽  
Lysosomal Enzymes ◽  
Mitochondrial Enzymes ◽  
Lysosomal Hydrolases ◽  
Serum Activity ◽  
Highly Correlated ◽  
Enzymatic Changes ◽  
Increased Activity

Abstract In each of 10 highly hyperglycemic decompensated diabetics with ketoacidosis, we found a markedly increased serum activity of two lysosomal hydrolases (N-acetyl-β-glucosaminidase and β-glucuronidase). This was also true to a lesser degree of five diabetics with less severe decompensation and without ketoacidosis. The activity of both enzymes and the degree of hyperglycemia were highly correlated. We think these enzymatic changes result from a process of activation and release of tissue lysosomal enzymes, probably occurring in connection with the increased catabolism present in decompensated diabetes. Nonlysosomal (cytoplasmic or mitochondrial) enzymes were less changed (aspartate and alanine aminotransferases) or normal (aldolase, lactate- and malate dehydrogenase, and creatine kinase). This indicates that tissue damage alone could not account for the increased activity of the two lysosomal hydrolases; it therefore seems primarily to be due to involvement of lysosomes.

Malate dehydrogenase: Isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms

1981 ◽  
Vol 1 (6) ◽  
pp. 497-507 ◽  
Author(s):  
Ross T. Fernley ◽  
Steven R. Lentz ◽  
Ralph A. Aradshaw
Keyword(s):  
Malate Dehydrogenase ◽  
Deae Cellulose ◽  
Mitochondrial Enzymes ◽  
Terminal Sequence ◽  
E Coli ◽  
Amino Terminal ◽  
Common Precursor ◽  
Polypeptide Chains ◽  
Mitochondrial Malate Dehydrogenase ◽  
Amino Terminal Sequence

Escherichia coli malate dehydrogenase has been isolated in homogeneous form by a procedure employing chromatography on DEAE-cellulose, 5′-AMP-Sepharose, and Sephacryl-200. It is composed of two identical polypeptide chains each of Mr = 32 500. Like porcine mitochondrial malate dehydrogenase, it is devoid of tryptophan, but otherwise it is not particularly more similar in composition to one of the eukaryotic isozymes than to the other. However, amino-terminal sequence analysis of the first 36 residues shows remarkable similarity of the bacterial and mitochondrial enzymes (69% identical residues) in contrast to the cytoplasmic form (27%). The two porcine heart enzymes are identical in 24t% of the positions compared. These results clearly establish that all three forms of malate dehydrogenase have evolved from a common precursor and that the prokaryotic and mitochondrial forms have retained sequences that are much closer to the ancestral one than the cytoplasmic enzyme. These findings appear to further substantiate the endosymbiotic hypothesis for the origin of the mitochondrion.

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

2000 ◽  
Vol 110 (3) ◽  
pp. 322-329 ◽  
Author(s):  
M. Miginiac-Maslow ◽  
K. Johansson ◽  
E. Ruelland ◽  
E. Issakidis-Bourguet ◽  
I. Schepens ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

SALT AND WATER BINDING TO HALOPHILIC MALATE DEHYDROGENASE

1984 ◽  
Vol 45 (C7) ◽  
pp. C7-269-C7-269
Author(s):  
G. Zaccai ◽  
E. Wachtel ◽  
H. Eisenberg
Keyword(s):  
Malate Dehydrogenase ◽  
Water Binding
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