Comparative Analysis of Glucosephosphate Isomerase, Lactate Dehydrogenase and Malate Dehydrogenase Isozymes in 9 Cyprinid Species from Italy.

1998 ◽  
Vol 15 (4) ◽  
pp. 461-467
Author(s):  
Sonia Manaresi ◽  
Barbara Mantovani ◽  
Francesco Zaccanti
Keyword(s):  
Comparative Analysis ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Glucosephosphate Isomerase ◽  
Cyprinid Species ◽  
Malate Dehydrogenase Isozymes

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 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.

Concurrent measurements of carcinoembryonic antigen, glucosephosphate isomerase, gamma-glutamyltransferase, and lactate dehydrogenase in malignant, normal adult, and fetal colon tissues.

1980 ◽  
Vol 26 (13) ◽  
pp. 1809-1812 ◽  
Author(s):  
D D Munjal
Keyword(s):  
Colon Cancer ◽  
Lactate Dehydrogenase ◽  
Carcinoembryonic Antigen ◽  
Tumor Tissue ◽  
Human Colon ◽  
Normal Adult ◽  
Metastatic Colon Cancer ◽  
Glucosephosphate Isomerase ◽  
Adult Human ◽  
Fetal Organs

Abstract Carcinoembryonic antigen and activities of glucosephosphate isomerase (EC 5.3.1.9), γ-glutamyltransferase (EC 2.3.2.2), and lactate dehydrogenase (EC 1.1.1.27) were measured in aqueous extracts of fetal, normal adult, and malignant human colon tissues. Fetal colon, as well as primary and metastatic colon tumor tissue, showed higher activities of these analytes than did normal adult human colon. Liver metastases of colon cancer gave the highest values, normal adult human colon the lowest. Statistically, these differences were more striking in the case of carcinoembryonic antigen and glucosephosphate isomerase than for γ-glutamyltransferase or lactate dehydrogenase. In contrast to the other markers, γ-glutamyltransferase activity was lower in fetal organs than in normal adult colon and colon tumors. These results are consistent with earlier observations that activities of these markers are significantly increased in the blood of patients with metastatic colon cancer.

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.

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