scholarly journals The putative l-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent l-malate dehydrogenase

2000 ◽  
Vol 37 (6) ◽  
pp. 1515-1520 ◽  
Author(s):  
Dominique Madern
Keyword(s):  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Methanococcus Jannaschii

scholarly journals Four Weeks of Aerobic Training Affects Cardiac Tissue Matrix Metalloproteinase, Lactate Dehydrogenase and Malate Dehydrogenase Enzymes Activities, and Hepatorenal Biomarkers in Experimental Hyperhomocysteinemia in Rats

2021 ◽  
Vol 22 (13) ◽  
pp. 6792
Author(s):  
Dusan Todorovic ◽  
Marija Stojanovic ◽  
Ana Medic ◽  
Kristina Gopcevic ◽  
Slavica Mutavdzin ◽  
...  
Keyword(s):  
Physical Activity ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Subcutaneous Injection ◽  
Cardiac Tissue ◽  
Albino Rats ◽  
Wistar Albino Rats ◽  
And Control ◽  
Tissue Matrix ◽  
Increased Activity

The aim of this study was to investigate the effect of the application of homocysteine as well as its effect under the condition of aerobic physical activity on the activities of matrix metalloproteinases (MMP), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) in cardiac tissue and on hepato-renal biochemical parameters in sera of rats. Male Wistar albino rats were divided into four groups (n = 10, per group): C: 0.9% NaCl 0.2 mL/day subcutaneous injection (s.c.); H: homocysteine 0.45 µmol/g b.w./day s.c.; CPA saline (0.9% NaCl 0.2 mL/day s.c.) and a program of physical activity on a treadmill; and HPA homocysteine (0.45 µmol/g b.w./day s.c.) and a program of physical activity on a treadmill. Subcutaneous injection of substances was applied 2 times a day at intervals of 8 h during the first two weeks of experimental protocol. Hcy level in serum was significantly higher in the HPA group compared to the CPA group (p < 0.05). Levels of glucose, proteins, albumin, and hepatorenal biomarkers were higher in active groups compared with the sedentary group. It was demonstrated that the increased activities of LDH (mainly caused by higher activity of isoform LDH2) and mMDH were found under the condition of homocysteine-treated rats plus aerobic physical activity. Independent application of homocysteine did not lead to these changes. Physical activity leads to activation of MMP-2 isoform and to increased activity of MMP-9 isoform in both homocysteine-treated and control rats.

Effect of thermal injury on the TCA cycle enzymes of Staphylococcus aureus MF 31 and Salmonella typhimurium 7136

1971 ◽  
Vol 17 (6) ◽  
pp. 759-765 ◽  
Author(s):  
Richard I. Tomlins ◽  
Merle D. Pierson ◽  
Z. John Ordal
Keyword(s):  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Thermal Injury ◽  
Specific Activity ◽  
Fumarate Hydratase ◽  
Tca Cycle ◽  
Tca Cycle Enzymes ◽  
The Tca Cycle ◽  
Oxoglutarate Dehydrogenase ◽  
Metabolic Activities

The heating of S. aureus MF-31 and S. typhimurium 7136 at 52C and 48C respectively, produced a sublethal heat injury. When injured cells were placed in fresh growth medium they recovered. The recovery of S. aureus was not inhibited by chloramphenicol. The metabolic activities of tricarboxylic acid (TCA) cycle enzymes, as well as other selected enzymes in crude extracts of normal and heat-injured cells of both microorganisms were assayed. In extracts from S. typhimurium there was some loss of specific activity with fumarate hydratase, glutamate dehydrogenase, fructose diphosphate aldolase, lactate dehydrogenase, and the NAD(P) oxidases as a result of heating. In extracts from S. aureus oxoglutarate dehydrogenase, malate dehydrogenase and lactate dehydrogenase were severely inactivated after heating. Other enzymes in comparison were only moderately sensitive to heat. No significant increase in enzyme activity was observed in extracts from injured cells of either microorganism. Re-naturation of lactate dehydrogenase and malate dehydrogenase occurred during the recovery of S. aureus both in the presence and absence of chloramphenicol. No renaturation of oxoglutarate dehydrogenase was found under the same conditions.

scholarly journals MALATE DEHYDROGENASE ISOZYMES OF THE CHICK EMBRYO

1965 ◽  
Vol 13 (6) ◽  
pp. 510-514 ◽  
Author(s):  
JAMES L. CONKLIN ◽  
EDWARD J. NEBEL
Keyword(s):  
Lactate Dehydrogenase ◽  
Chick Embryo ◽  
Malate Dehydrogenase ◽  
Molecular Basis ◽  
Specific Pattern ◽  
Starch Gel Electrophoresis ◽  
Organ Specific ◽  
Malate Dehydrogenase Isozymes ◽  
Starch Gel ◽  
Mitochondrial Malate Dehydrogenase

Malate dehydrogenase fractions of the chick embryo were demonstrated after starch gel electrophoresis of homogenates of liver, brain and spleen. A total of seven malate dehydrogenase fractions were observed to occur in the chick embryo in an organ specific pattern. Treatment of the homogenates with urea, sodium chloride-sodium phosphate, and p-chloromercuribenzoate prior to electrophoresis revealed that only three distinct malate dehydrogenase-active proteins were presence. Two of these proteins exhibited properties similar to those previously reported for the supernatant malate dehydrogenase and mitochondrial malate dehydrogenase of other species. Becuase of the differing properties of chick malate and lactate dehydrogenase it is concluded that the molecular basis for malate dehydrogenase isozymes is different from that reported for lactate dehydrogenase isozymes.

Lactate Dehydrogenase and Malate Dehydrogenase of Sertoli Cells in Rats

1987 ◽  
Vol 19 (1) ◽  
pp. 59-64 ◽  
Author(s):  
V. Santiemma ◽  
V. Salfi ◽  
N. Casasanta ◽  
A. Fabbrini
Keyword(s):  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Sertoli Cells

Automated Kinetic Spectrophotometric Assays of Enzyme Activities of Human Cerebrospinal Fluid: Methods and Reference Values

1973 ◽  
Vol 19 (2) ◽  
pp. 240-247 ◽  
Author(s):  
David M Sharpe ◽  
A Ross Wilcock ◽  
David M Goldberg
Keyword(s):  
Cerebrospinal Fluid ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Reference Values ◽  
Major Effect ◽  
Aspartate Transaminase ◽  
Exogenous Enzyme ◽  
Human Cerebrospinal Fluid ◽  
Upper Limits ◽  
Kinetic Spectrophotometric

Abstract Optimum conditions with respect to pH and molarity of phosphate buffer, and the concentrations of substrates, coenzymes, and exogenous enzyme, were defined at 37°C for activity of aspartate transaminase and lactate dehydrogenase of human cerebrospinal fluid (CSF), as measured by optical kinetic assays at 340 nm. The resulting methods, and a previously published procedure for malate dehydrogenase activity applicable to human CSF, were adapted for use with an automatic reaction-rate monitor. Within-batch and between-batch precision of all methods was satisfactory, and repeated estimations in seven subjects showed good agreement. Freezing samples decreased their activity by 5 to 10%, but thereafter no further losses occurred at -20°C for as long as three months. Injection of up to 12 ml of air during encephalography had no major effect. Reference values, derived from subjects with no neurological or simple chronic degenerative CNS disease, suggested that the upper limits (in U/liter) are: aspartate transaminase, 13.5; lactate dehydrogenase, 40; malate dehydrogenase, 58.

Kinetics of Thyroid Hormone Induced Changes in Liver and Skeletal Muscle Enzymes of Clarias batrachus

1999 ◽  
Vol 54 (5-6) ◽  
pp. 458-462 ◽  
Author(s):  
G. Tripathi
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Metabolic Enzymes ◽  
Time Dependent ◽  
Clarias Batrachus ◽  
Muscle Enzymes ◽  
Induced Changes ◽  
Kinetics Of ◽  
Mitochondrial Malate Dehydrogenase

Abstract Kinetics of triiodothyronine (T3) induced changes were studied in cytoplasmic malate dehydrogenase (cMDH), mitochondrial malate dehydrogenase (mMDH) and lactate dehydrogenase (LDH) of the liver and skeletal muscle of a catfish, Clarias batrachus. The rates of gradual inductions in the activities of all the three metabolic enzymes were faster in skeletal muscle than those of the liver. These time-dependent and tissue-specific inductions may be due to the possible differences in the rates of different enzymic syntheses. The maximum inductions in the activities of cMDH, mMDH and LDH were recorded around 19 hr after T3 treatment. Thereafter, the activities of all the enzymes gradually declined to their half levels within the next 12 hr which reflected the physiological half-life of these metabolic enzymes in the freshwater catfish.

pH-mediated control of anti-aggregation activities of cyanobacterial and E. coli chaperonin GroELs

2020 ◽  
Author(s):  
Tahmina Akter ◽  
Hitoshi Nakamoto
Keyword(s):  
Escherichia Coli ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Citrate Synthase ◽  
Ph Dependence ◽  
Chaperone Activity ◽  
Ph Change ◽  
Aggregation Assay ◽  
E Coli ◽  
Aggregation Activity

Abstract In contrast to Escherichia coli, cyanobacteria have multiple GroELs, the bacterial homologues of chaperonin/Hsp60. We have shown that cyanobacterial GroELs are mutually distinct and different from E. coli GroEL with which the paradigm for chaperonin structure/function has been established. However, little is known about regulation of cyanobacterial GroELs. This study investigated effect of pH (varied from 7.0 to 8.5) on chaperone activity of GroEL1 and GroEL2 from the cyanobacterium Synechococcus elongatus PCC7942 and E. coli GroEL. GroEL1 and GroEL2 showed pH dependency in suppression of aggregation of heat-denatured malate dehydrogenase, lactate dehydrogenase and citrate synthase. They exhibited higher anti-aggregation activity at more alkaline pHs. Escherichia coli GroEL showed a similar pH-dependence in suppressing aggregation of heat-denatured lactate dehydrogenase. No pH dependence was observed in all the GroELs when urea-denatured lactate dehydrogenase was used for anti-aggregation assay, suggesting that the pH-dependence is related to some denatured structures. There was no significant influence of pH on the chaperone activity of all the GroELs to promote refolding of heat-denatured malate dehydrogenase. It is known that pH in cyanobacterial cytoplasm increases by one pH unit following a shift from darkness to light, suggesting that the pH-change modulates chaperone activity of cyanobacterial GroEL1 and GroEL2.

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