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Results for “MALATE DEHYDROGENASE”

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PubMedDate not supplied

[Isoenzyme spectrum of lactate dehydrogenase, malate dehydrogenase, esterase and acid phosphatase of rat brain cells at different times after external 1 Gy gamma irradiation].

The influence of external single gamma-irradiation with a dose of 1 Gy on the isoenzyme composition of lactate dehydrogenase, malate dehydrogenase, esterase and acid phosphatase in the cytoplasm of rat brain cells has been investigated. Irradiation was shown to cause differently directed changes in the ratio of the isoenzymes under study at different times after exposure. The isoenzyme spectrum of lactate dehydrogenase and malate dehydrogenase was shown to be normalized on day 30 after irradiation, whereas the isoform composition of esterase and acid phosphatase was not stabilized at that time.

Acid Phosphatase↗

PubMed1988

Determination of the characteristics, properties and homogeneity of rat brain microsomes. Binding of lactate dehydrogenase, malate dehydrogenase and 5' nucleotidase to microsomal membranes.

Quantitatively, the amount of microsomes obtained using dimethyl sulfoxide is larger than that obtained from sucrose solutions (Centelles, Franco & Bozal (1986) Biol. Chem. Hoppe Seyler 367, 461-475). In this paper it is demonstrated that from a qualitative point of view they appeared to be indistinguishable with respect to molecular characteristics. Thus, both types of microsomes had the same behaviour in experiments of isopicnic ultracentrifugation with Percoll, isoelectric focusing and gel permeation. In these experiments, the 5'-nucleotidase, lactate dehydrogenase and malate dehydrogenase activities bound to the microsomal fraction were also studied. Lactate and malate dehydrogenase activities were always found in free and membrane-bound form. In contrast, 5'-nucleotidase activity was always encountered bound to microsomal membranes.

5'-Nucleotidase↗

PubMed1977

Influence of L-thyroxine upon enzymatic activity in the renal tubular epithelium of the rat under normal conditions and mercury-induced lesions. II. Histochemical studies of lactate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, unspecific esterase, and glucose-6-phosphate dehydrogenase.

Mercury-induced renal tubular lesions in the rat present histochemically with a decrease of succinate dehydrogenase (SDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G-6-PD), and unspecific esterase (UE), but with an increase of lactate dehydrogenase (LDH), indicating a drop of energy supply as well as a switch from oxidative to glycolytic energy production. L-thyroxine has the same effect on SDH, G-6-PD, and LDH, but an inverse effect on MDH and UE, pointing to stimulation of gluconeogenesis. However, administration of L-thyroxine to animals which have been submitted to sublimate intoxication even further decreases the MDH and UE activity while raising or partly restoring the activity of LDH, SDH, and G-6-PD. This observation is interpreted as an attempt of the damaged epithelial cell, as the gluconeogenesis ceases, to gain relatively more energy supply for the benefit of the vitally indispensable tubular Na+ reabsorption.

Acute Kidney Injury↗

PubMed1989

The isozymes of lactate dehydrogenase, malate dehydrogenase and glucosephosphate isomerase in Italian ictalurids.

1. The isozymes of lactate dehydrogenase (LDH), malate dehydrogenase (MDH) and glucose-phosphate isomerase (GPI) of three species of Italian ictalurids: Ictalurus sp., I. nebulosus marmoratus, and I. punctatus, were analyzed. 2. Isoelectric focusing (IEF) was applied to polyacrylamide gel plates, and the isozymes revealed by means of specific histochemical staining. 3. Species-specific monomorphic patterns were found for LDH. 4. In contrast, MDH and GPI have the same patterns in I. sp. and I. nebulosus marmoratus and different patterns in I. punctatus. 5. Comparison of the isozymatic patterns of the three species clearly showed the close relationship between I. sp. and I. nebulosus marmoratus and the relative taxonomic distance of I. punctatus, and thus the early detachment of this last species from a presumptive common ancestral lineage.

Animals↗

PubMed1995

Isoenzyme patterns of glucose-6-phosphate dehydrogenase, malate dehydrogenase and lactate dehydrogenase in Babesia rodhaini and Babesia microti.

Glucose-6-phosphate dehydrogenase (G6PD), malate dehydrogenase (MDH), and lactate dehydrogenase (LDH) activities and their isoenzyme patterns in B. rodhaini (BR) and B. microti (BM), the two major causative species of murine babesiosis, were examined. G6PD and LDH activities were higher in BR than those in BM, whereas MDH activity was lower in BR than that in BM. No differences were observed between BR and BM in the mobility of isoenzyme bands of G6PD and MDH. On LDH isoenzyme pattern, at least 5 bands were detected in BR, while only one band in BM. Since each subunit of LDH is known to be coded by different gene, these results suggests that BR and BM are able to be differentiated genetically.

Animals↗

PubMed1982

Rat liver L-glutamate dehydrogenase, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and sulfite oxidase are each synthesized as larger precursors by cytoplasmic free polysomes.

Four cytoplasmically synthesized rat liver mitochondrial enzymes, located either as soluble enzymes in the mitochondrial matrix (L-glutamate dehydrogenase and malate dehydrogenase or in the intermembrane space (sulfite oxidase) or as an integral membrane protein located on the matrix face of the inner mitochondrial membrane (D-beta-hydroxybutyrate dehydrogenase), were all shown to be synthesized as precursors larger than their mature counterparts by 1000-6000 daltons. These larger forms were detected in vitro, in a cell-free protein synthesizing system programmed with either total rat liver RNA or with RNA isolated from free polysomes or with free polysomes, and in vivo, in the two cases that were investigated (L-glutamate dehydrogenase and D-beta-hydroxybutyrate dehydrogenase), by pulse labeling of Buffalo rat liver cells in culture. The intracellular site of synthesis of all four mitochondrial enzymes was shown to be primarily on free polysomes and not on membrane-bound polysomes.

Animals↗

PubMed1989

Some aspects of isozymes of lactate dehydrogenase, malate dehydrogenase and glucosephosphate isomerase in fish.

1. The present paper reports some aspects of the isozymes of LDH, MDH and GPI in fish. 2. In Petromyzontiformes LDH is encoded by a single Ldh-A gene locus. In Myxiniformes and in most vertebrates LDH is encoded by two gene loci, A and B. A third Ldh-C locus is characteristic of the bony fishes Actinopterygii. 3. In fish the MDH isozymes are generally encoded by three gene loci Mdh-M, Mdh-A and Mdh-B. 4. In most diploid bony fish the GPI is controlled by two independent gene loci Gpi-A and Gpi-B. 5. The relationships of isozymes with evolution of vertebrates, tissual specificity, ontogenetic changes, with physiological and metabolic roles are discussed.

Animals↗

PubMed1977

The frequency in Japanese of genetic variants of 22 proteins II. Carbonic anhydrase I and II, lactate dehydrogenase, malate dehydrogenase, nucleoside phosphorylase, triose phosphate isomerase, haemoglobin A and haemoglobin A2.

This paper presents the results of a survey of Japanese for electrophoretic variants of CA I, CA II, LDH, MDH, TPI, NP, HB A and A2, the number of determinations per system ranging from 738 to 4029. Four similar variants of CA I (designed CA IHIR1), one of LDH (designated LDHNGS1), one of MDH (designated MDHS 7HIR1), two of HB A (one a reascertainment of HB Hijiyama, the other not characterized), and one characterized by the absence of HB A2 (delta-thalassaemia) were observed and are described. The CA IHIR1, LDHNAG1 and MDHS 2HIR1 variants have not been previously observed in Japan. No electrophoretic variants were found in the TPI and NP systems.

Adult↗

PubMedDate not supplied