Comparison of the kinetic behaviour of lactate dehydrogenase and cytosolic and mitochondrial malate dehydrogenase from guinea pig skeletal muscle

1990 ◽  
Vol 58 (2) ◽  
pp. 269-275 ◽  
Author(s):  
A. Mazo ◽  
J.Ll. Gelpí ◽  
A. Cartés
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Guinea Pig ◽  
Malate Dehydrogenase ◽  
Kinetic Behaviour ◽  
Mitochondrial Malate Dehydrogenase

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.

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.

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 Changes in lactate dehydrogenase and malate dehydrogenase activities during hypoxia and after temperature acclimation in the armored fish, Rhinelepis strigosa (Siluriformes, Loricariidae)

2000 ◽  
Vol 60 (2) ◽  
pp. 353-360 ◽  
Author(s):  
L. PANEPUCCI ◽  
M. N. FERNANDES ◽  
J. R. SANCHES ◽  
F. T. RANTIN
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
White Muscle ◽  
Acute Hypoxia ◽  
Temperature Acclimation ◽  
Muscle Enzyme ◽  
First Time ◽  
Substrate Concentrations ◽  
Muscle Enzyme Activities

Lactate (LDH) and malate dehydrogenase (MDH) of white skeletal muscle of fishes acclimated to 20, 25 and 30°C and thereafter submitted to hypoxia were studied in different substrate concentrations. Significant differences for LDH and MDH of white muscle enzyme activities are described here for the first time in Rhinelepis strigosa of fishes acclimated to 20°C and submitted to hypoxia for six hours. LDH presented a significant decrease in enzyme affinity for pyruvate in acute hypoxia, for fishes acclimated to 20°C and an increase for fishes acclimated to 30°C.

Control of enzyme activities in individual myotubes cultured without nerve

1985 ◽  
Vol 249 (3) ◽  
pp. C313-C317 ◽  
Author(s):  
P. M. Nemeth ◽  
L. Solanki ◽  
J. C. Lawrence
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Adenylate Kinase ◽  
Contractile Activity ◽  
Primary Cultures ◽  
Rat Skeletal Muscle

The activities of lactate dehydrogenase, malate dehydrogenase, phosphorylase, and adenylate kinase were measured in single myotubes dissected from primary cultures of rat skeletal muscle. For a given enzyme, activities among the spontaneously contracting cells varied as much as eightfold. When the myotubes were paralyzed with tetrodotoxin, the variability in enzyme levels was markedly decreased. These and other findings suggest that differences in enzyme levels among individual myotubes may arise as a result of differences in their pattern of contractile activity.

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