PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “GLYCEROLPHOSPHATE DEHYDROGENASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 145 records · Page 8Linked to original sources
PubMed1983

Histochemical studies of acid proteoglycans and glycoproteins and activities of hydrolytic and oxidoreductive enzymes in the skin epidermis of the fish Blennius sanguinolentus pallas (Teleostei: Blenniidae).

In the epidermis of the fish Blennius sanguinolentus the histochemistry of complex carbohydrates and various oxidoreductases has been studied by means of a series of selected light microscopical techniques. The epidermis is endowed with three types of secretory cells namely, the mucous goblet cells, the superficial polygonal cells and the ionocytes, which provide protective functions in view of their involvement in the prevention of the skin epithelium from invading pathogens and in the osmoregulation processes respectively. The secretory substances of mucous goblet cells contain sulfated, carboxylated and neutral complex carbohydrates in addition to a glycoprotein with sialic acid terminal to galactose in its oligosaccharide chains. Activities of SDH, ICDH, MDH and G-6-PDH were studied, to elucidate some aspects of the correlated functions of the ionocytes which play a key role in the performance of the maintenance of the electrolyte pattern in the internal milieu of the skin. Differences in the intensity of various oxidoreductases are correlated with the extent of the activity of the epidermis for related to secretion of a mucous cover over the surface. Activity of the oxidoreductases is confined mainly to the basal and outer epidermal layers and this enzyme zonation is discussed with reference to the existence of the high turnover rate of the epithelial cells and both the proliferative and respiratory capabilities of the skin epithelium.

Alkaline Phosphatase↗
PubMed1983

Metabolic variation among rat lumbosacral alpha-motoneurons.

Despite the wealth of literature concerned with muscle fiber biochemical, ultrastructural and physiological characteristics, little information is available regarding the metabolic enzyme activities of alpha-motoneurons. The present study examines the metabolism of alpha-motoneurons located in the lateral cell column of the rat lumbosacral enlargment with a quantitative histochemical technique. Variation in the activities of alpha-glucan phosphorylase, NADH-diaphorase, succinic dehydrogenase and acid phosphatase were detectable with the photographic densitometry and atomic absorption spectrophotometry technique. No difference in the glycolytic enzyme activity (mitochondrial alpha-glycerophosphate dehydrogenase) was observed. Analysis of lactate dehydrogenase isoenzymes demonstrated the existence of H type isoenzyme in alpha-motoneurons, consistent with other observations indicating predominance of aerobic metabolism within these neurons. The activities of the former enzymes in alpha-motoneurons formed a complete spectrum of activities, distributed unimodally. Smaller motoneurons exhibited the greatest NADH-D and acid phosphatase activities; phosphorylase activity was greatest in larger motoneurons. Significant variation in the enzyme activity of similar-sized motoneurons suggests that the metabolism of the motoneuron is regulated by factors other than cell size. Relationships between motoneuron metabolic enzyme activity and motor unit type are under current investigation.

Acid Phosphatase↗
PubMedDate not supplied

Polyacrylamide gel technique for the histochemical demonstration of soluble enzymes.

Soluble enzymes were immobilized and visualized by polyacrylamide gel slabs, impregnated with the incubation medium including auxiliary enzymes. The method has several advantages over existing techniques which make use of gel films or a semipermeable membrane. The diffusion of tissue compounds is effectively limited, while auxiliary enzymes may be operative. Moreover the viscosity of the medium is temperature-independent so that the incubation temperature can be varied. To demonstrate the suitability of the method glycerol-3-phosphate dehydrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphoglucomutase and aldolase were visulaized in human or rat skeletal muscle. Cytosolic and mitochondrial glycerol-3-phosphate dehydrogenase were both visualized in the absence of added NAD+ and menadione. For the visualization of ATP producint enzymes, like creatine kinase and pyruvate kinase, the method is not suitable.

Animals↗
PubMed1991

Electrophoretic variation at flight-related enzyme loci and its possible association with flight capacity in Epiphyas postvittana.

Variations at three flight-related enzyme loci, delta-glycerophosphate dehydrogenase (delta-Gpdh), glucose-6-phosphate dehydrogenase (G6pd), and phosphoglucomutase (Pgm), of Epiphyas postvittana (Walker) moths were investigated using starch gel electrophoresis. Among the three enzyme loci, delta-Gpdh and G6pd were found to be monomorphic, but Pgm was polymorphic, with a total of seven different genotypes and five alleles identified in this study. Comparisons of allozyme variability at the Pgm locus showed significant differentiation among five natural populations sampled from geographically distinct localities in New Zealand and Australia and between laboratory populations differentiated by artificial selection on flight capacity. The Pgm polymorphism was shown to be associated with the variation of flight capacity, but the role of the enzyme locus in the evolution of flight behavior is to be demonstrated in this species.

Animals↗
PubMed1993

Streptozotocin-induced FAD-glycerophosphate dehydrogenase suppression in pancreatic islets. Relationship with the severity and duration of hyperglycaemia and resistance to insulin or riboflavin treatment.

In vitro, streptozotocin (1.0-2.0 mM) fails to exert any immediate effect on the activity of FAD-glycerophosphate dehydrogenase in either pancreatic islet homogenate or freshly isolated intact islets. However, when injected in vivo, streptozotocin (40 mg/kg body weight) lowers the specific activity of the FAD-linked enzyme in islet homogenates within 24 h, whilst causing little change in 2-ketoglutarate dehydrogenase and increasing glutamate dehydrogenase islet activity. In animals which became frankly hyperglycaemic as the result of the injection of streptozotocin, the activity of islet FAD-glycerophosphate dehydrogenase, measured 2 weeks after administration of the B-cell cytotoxic agent, was decreased to 10-20% of its control value. Neither insulin treatment nor riboflavin supplementation affected this enzymic defect. Even when the animals injected with streptozotocin remained virtually euglycaemic, the activity of islet FAD-glycerophosphate dehydrogenase was markedly decreased. This coincided with a preferential impairment of aerobic glycolysis, as judged from the ratio between D-[3,4-14C]glucose oxidation and D-[5-3H] glucose utilization by the islets. It is proposed, therefore, that the administration of sub-diabetogenic amounts of streptozotocin to adult rats represents an alternative and easier approach to the study of B-cell dysfunction in this model of type 2 (non-insulin-dependent) diabetes than does streptozotocin injection in neonatal rats.

Alloxan↗
PubMed1976

Enzyme activity patterns of energy supplying metabolism in the quadriceps femoris muscle (vastus lateralis): sedentary men and physically active men of different performance levels.

1. In 3 groups of men, differing as to the amount and intensity of physical training loads, increasing in the order "sedentary": "sporting": "athletic", enzyme activities were estimated in biopsy samples of m. quadriceps femoris (vastus lateralis). The enzymes were: Hexokinase (HK), NAD: glycerol-3-phosphate dehydrogenase (GPDH), triosephosphate dehydrogenase (TPDH), lactate dehydrogenase (LDH), citrate synthase (CS), NAD: malate dehydrogenase (MDH), and 3-hydroxyacyl-CoA dehydrogenase (HOADH). Indicators of laboratory performance and whole-body metabolic capacities (maximal oxygen consumption etc.) were estimated in the "sporting" and "athletic" groups. 2. In the 2 latter groups, distinguished by greater physical activity, the atypical enzyme activity pattern, remarkable by a low activity of LDH and high relative activities of GPDH and HK, as reported earlier in a sedentary group (Bass et al., 1975a), disappeared. The possibility of the atypical low LDH enzyme activity pattern as resulting from lack of bodily exertion is discussed. 3. The moderately trained "sporting" group distinguishes itself from the "sedentary" one mainly by a higher activity of LDH and by lower activities of GPDH and MDH. In the intensively trained "athletic" group, enzymes connected to aerobic oxidation (MDH, CS, HOADH) and GPDH also show higher activities than in the "sporting" group. The difference between the two more active groups is further borne out by a higher maximum oxygen uptake and carbon dioxide release of the well-trained "athletic" group. This difference of enzyme activity pattern may not be confined to the quadriceps femoris muscle.

Adult↗
PubMed1975

M. Quadriceps femoris of man, a muscle with an unusual enzyme activity pattern of energy supplying metabolism in mammals.

1. The following enzyme activities were estimated in needle-biopsy samples of the lateral part of the human quadriceps femoris muscle: triosephosphate dehydrogenase (TPDH), lactate dehydrogenase (LDH), NAD : glycerol-3-phosphate dehydrogenase (GPDH), hexokinase (HK), NAD: malate dehydrogenase (MDH), citrate synthase (CS) and hydroxyacyl-CoA dehydrogenase. 2. Although the enzyme activities in muscles of women were lesser than in those of men, no difference was found in the calculated enzyme activity ratios. There is thus no sex-dependent metabolic type-differentiation in this muscle. 3. The human quadriceps femoris is a low-activity muscle, in comparison with muscles of homoiotherm laboratory animals. The enzyme activity ratio of TPDH to CS, characterizing the glycolytic pyruvate formation to aerobic oxidative capacities, shows this muscle to be of an intermediate type in this respect, similarly as the extensor digitorum longus of the rat. The relatively very high capacity of glucose phosphorylation (HK), the high aerobic regeneration of cytoplasmic dehydrogenated NAD (GPDH) and the very low anaerobic regeneration (LDH), show the unusually high proportion of carbohydrates (glucose) which can be broken down aerobically.

Acetyl Coenzyme A↗