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.

scholarly journals Selective permeability of rat liver mitochondria to purified malate dehydrogenase isoenzymes in vitro

1980 ◽  
Vol 192 (2) ◽  
pp. 649-658 ◽  
Author(s):  
S Passarella ◽  
E Marra ◽  
S Doonan ◽  
E Quagliariello
Keyword(s):  
Malate Dehydrogenase ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Enzymic Activity ◽  
Rat Liver Mitochondria ◽  
Starch Gel Electrophoresis ◽  
Selective Permeability ◽  
Starch Gel ◽  
Mitochondrial Malate Dehydrogenase

1. The mitochondrial malate dehydrogenase from rat liver has been purified to a state of homogeneity as judged by starch-gel electrophoresis and the cytoplasmic isoenzyme has been obtained in a partically purified state. 2. Inhibition of the isoenzymes by sulphite has been studied. 3. In mitochondria loaded with sulphite, the catalytic activity of the (partially inhibited) internal malate dehydrogenase has been measured by addition of oxaloacetate to the suspension medium and observation of the consequent decrease in fluorescence of NADH. 4. Addition of mitochondrial malate dehydrogenase to suspensions of mitochondria loaded with sulphite resulted in an increase in the level of intramitochondrial enzymic activity as measured by the above technique. Addition of the cytoplasmic isoenzyme did not result in such an increase. 5. These results show that mitochondria in suspension are permeable to the mitochondrial malate dehydrogenase but not to the cytoplasmic isoenzyme. 6. This conclusion has been confirmed by direct measurement of a decrease of enzyme activity in solution and an increase inside the mitochondria after incubation of organelles in solutions containing mitochondrial malate dehydrogenase. No such effect was observed with the cytoplasmic isoenzyme. 7. Some features of the permeation process have been studied.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

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.

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 The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

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.

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

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