Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle

1977 ◽  
Vol 52 (3) ◽  
pp. 201-206 ◽  
Author(s):  
Cornelia Spamer ◽  
Dirk Pette
Keyword(s):  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Soleus Muscle ◽  
Activity Patterns ◽  
Rabbit Psoas ◽  
Glyceraldehydephosphate Dehydrogenase

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

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

2004 ◽  
Vol 97 (4) ◽  
pp. 1424-1430 ◽  
Author(s):  
Tyrone A. Washington ◽  
James M. Reecy ◽  
Raymond W. Thompson ◽  
Larry L. Lowe ◽  
Joseph M. McClung ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Soleus Muscle ◽  
High Energy ◽  
Northern Blotting ◽  
Mrna Abundance ◽  
Hindlimb Suspension ◽  
Sprague Dawley ◽  
Muscle Lactate ◽  
Rat Soleus Muscle

Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372%, and LDH-B mRNA abundance decreased by 43 and 31% after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80% after 3 days of functional overload. Additionally, LDH-A activity increased by 234% following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.

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.

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