The influence of fasting and pancreatectomy on some glycolytic enzymes in the muscle of garden lizard, Calotes versicolor.

The leg muscle of Calotes versicolor consists mainly of white fibers. They can be classified into small, intermediate and broad fibers according to their diameter and staining reaction. The histochemical study of some of the glycolytic enzymes such as aldolase, phosphorylase, lactic dehydrogenase (LDH) and alpha-glycerophosphate dehydrogenase (alpha-GPDH) is described in the muscle of normal, pancreactomized and insulin injected animals. Highest activity of all enzymes was observed in the small fibers, though they occur in negligiable amount (3%). The intermediate and broad fibers exhibited medial and lowest activities respectively. 24 h after the extirpation of the pancreas a considerable inhibition is noted in the activities of phosphorylase, LDH and alpha-GPDH. Induced inanition for 21 days ensued insignificant but gradual decrease and increase in the alpha-GPDH and phosphorylase activities respectively in both unoperated and operated animals. The aldolase shows its mere presence in normal and trace activity in pancreatectomized animals. The injection of insulin (40 i.u./kg) at the interval of 30 min, 60 min, 4 h, 12 h and 24 h is given. The activities of all enzymes is stimulated at 30 min and depleted 4 h after the injection. The level of activity was remaintained at 12 h to 24 h stage. The possible physiological role and significance of enzymes in the synthesis and breakdown of glycogen is discussed.     

Glycolytic enzymes in the premolt field crab Paratelphusa hydrodromus (Milne-Edwards) (Crustacea)

The quantitative assay of hexokinase (HK), phosphorylase, phosphofructokinase (PFK), glucose 6-phosphate dehydrogenase (G-6-PDH), glycerol 3-phosphate dehydrogenase (G-3 PDH) and lactate dehydrogenase (LDH) revealed that coxal muscles compared to hepatopancreas contained higher activities of all the enzymes investigated. It appears that the coxal muscles of the premolt field crab has carbohydrate-based fuel economy. The hepatopancreas is a rich source of lipid and very poor source of glycogen. The activity of G-6-PDH is moderately high in the hepatopancreas. It seems that in this lipogenic tissue conversion of G-6-P to triose phosphate occurs predominately via pentose-phosphate pathway thus generating NADPH for lipogenesis. The relative G-3PDH ad LDH activities in hepatopancreas and coxal muscles led us to believe that the reconversion of NAD from NADH in hepatopancreas nd muscle flexor is effected by glycerol 3-phosphate shuttle, whereas in muscle extensor it is achieved by both G-3PDH and LDH activities.     

Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata).

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.     

Effect of tuftsin on enzyme activity in the energy metabolism of lymphocytes

The cytochemical technique was used to measure the activity of succinate dehydrogenase (SDH), lactate dehydrogenase (LDH) and glucose-6-phosphate dehydrogenase (G-6-PDH) of peripheral blood lymphocytes of mice and rats given intraperitoneal injections of an endogenous immunostimulant tuftcin (Tre-Lys-Pro-Arg) in a dose of 0.3 mg/kg. A significant decrease of SDH activity was observed both in mice and rats 4 and 6 hours following injection, respectively. In mice, that activity returned to normal in 12, while in rats in 24 hours. An opposite action was produced by tuftcin on G-6-PDH, causing the maximum elevation of the enzyme activity in rat lymphocytes 6 hours after peptide administration. The decrease to the initial level was observed in 24 hours. Tuftcin did not affect the activity of LDH. The data obtained indicate that the immunological effect of tuftcin is coupled with the changes in the activity of Krebs cycle enzymes (SDH) and pentose phosphate cycle enzymes (G-6-PDH).     

Enzymatic activity in crude oil contaminated rats

The activity of enzymes found in the plasma, malate dehydrogenase (MDH) and lactate dehydrogenase (LDH), and enzymes from erythrocytes, glucose-6-phosphate dehydrogenase (G-6-PDH) and catalase, was studied in rats contaminated by crude oil. Crude oil (tube fed) contamination caused a significant increase in MDH and LDH activity 96 hr after contamination while a decrease in activity was noted in 6-6-PDH and catalase. An additional contamination (1 week after the first contamination), measured 96 hr after contamination, caused a relative decrease in MDH and LDH activity while there was a contrasting relative increase in G-6-PDH and catalase activity. After a recovery period of 3 weeks the only significant change was an increase in catalase activity.     

Histochemical localization of glycogen and some representative enzymes of glycolytic cycle in the cheliped muscle of Scylla serrata (Forskal) (Brachyura: Decapoda)

Glycogen, phosphorylase, aldolase, a-glycerophosphate dehydrogenase, lactic dehydrogenase and glucose-6-phosphate dehydrogenase were localized histochemically in the cheliped muscle of Scylla serrata (Forskal) in normal, destalked, destalked receiving eyestalk extract injection and intact injected with eyestalk extract.     

砷对兰州鲇组织中代谢酶活性及RNA和蛋白质含量影响

采用毒性试验方法,研究了安全浓度（1.288 mg/L）条件下亚砷酸钠（NaAsO2）对兰州鲇（Silurus lanzhouensis）脑、鳃、肝脏、肌肉4种组织中6-磷酸葡萄糖脱氢酶（G-6-PDH）和乳酸脱氢酶（LDH）活性,以及RNA和蛋白质含量的影响。结果表明,染毒21d时,As（Ⅲ）可显著降低4种组织中G-6-PDH和LDH活性、RNA和蛋白质含量（P0.05）。撤毒后21d,除脑和肝组织中蛋白质含量未恢复到对照组水平（P0.05）,肝脏中G-6-PDH活性超过了对照组水平（P0.05）外,其余各组织中G-6-PDH和LDH活性、RNA和蛋白质含量均可恢复到对照组水平（P0.05）。以上结果表明,As（Ⅲ）对兰州鲇组织中代谢酶活性具有明显的抑制作用,可致组织细胞RNA损伤和可溶性蛋白质减少,但这种影响是可逆的,撤毒后一定时间内可恢复到正常水平。       

Die Histotopik einiger Oxydoreduktasen im Hoden von Hund und Katze

Zusammenfassung Im Hoden von Hund und Katze werden folgende Enzyme histochemisch nachgewiesen: NADH-Tetrazoliumreduktase (NADH-T-Red), NADPH-Tetrazoliumreduktase (NADPH-T-Red), Cytochromoxydase (Cyt-Ox), Lactat-Dehydrogenase (LDH), Aldolase (ALD), Alkohol-Dehydrogenase (ADH), Glycerin-1-phosphat-Dehydrogenase (GDH), Glucose-6-phosphat-Dehydrogenase (G-6-PDH), Succinat-Dehydrogenase (SDH), NAD-spezifische Isocitrat-Dehydrogenase (NAD-ICDH). Die starke Fermentaktivität der G-6-PDH und der LDH in den Leydig-Zellen beider Spezies, der relativ hohe Gehalt an histochemisch nachweisbarer ADH in den Zwischenzellen der Katze sowie eine deutliche Reaktion auf GDH in den Sertoli-Zellen der Katze werden diskutiert.

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Summary In the testes of dog and cat the distribution pattern of NADH-tetrazolium reductase, NADPH-tetrazolium reductase, cytochrome oxydase, lactate dehydrogenase, aldolase, alcohol dehydrogenase, -glycerophosphate dehydrogenase, glucose-6-phosphate dehydrogenase, succinate dehydrogenase and NAD specific isocitrate dehydrogenase was studied by histochemical means. The strong reaction of G-6-PDH and LDH in the Leydig cells of both species, the relatively high amount of ADH in the interstitial cells of the cat testis and the principal site of -GPDH in the Sertoli cells of the cat are discussed.

     

Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases

Summary In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, nothing dehydrogenase reaction, use of exogenous CoQ₁₀ and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of l-glutamate dehydrogenase (E.C. 1.4.1.2 and E.C. 1.4.1.3) have been investigated in the rat cerebellum.It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ₁₀, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type.Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.     

Effect of tuftsin on the activity of energy metabolism enzymes in peritoneal macrophages

Cytochemistry was used to measure the activity of succinate dehydrogenase (SOD), lactate dehydrogenase (LDH) and glucose-6-phosphate dehydrogenase (G-6-PDH) in rat peritoneal macrophages under the action of the endogenous immunostimulant tuftcin (tre-lys-pro-arg) during phagocytosis of latex particles and at rest. Tuftcin did not affect the activity of the study enzymes in non-phagocytic cells. Elevation of the peptide concentration to 0.25 micrograms/ml and higher in phagocytic macrophages activated G-6-PDH and lowered the activity of LDH. Tuftcin did not alter the activity of SOD in phagocytic macrophages.     

Adrenal dehydrogenases in alloxan diabetic rats following continuous exposure to light

The enzymes delta5-3beta-hydroxysteroid dehydrogenase delta5-3beta-HSD) and glucose-6-phosphate dehydrogenase (G-6-PDH) were demonstrated histochemically in the adrenal cortex of female rat. The activities of these enzymes were increased significantly in the alloxan-treated rats kept in LD (light: darkness) cycles of 10:14 h. Continuous light exposure to diabetic animals appeared to decrease delta5-3beta-HSD and g-6-PDH in comparison to the diabetic rats kept in 10 h illumination. The evidence indicates that suppression of adrenal steroidogenesis in diabetic rats after exposure to continuous light is due to the alteration of pentose phosphate pathway.     

Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata).

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).     

Metabolic differentiation of homologous leg muscles of two aquatic birds at the level of enzymatic organization

The quantitative determination of succinic dehydrogenase (SDH), hexokinase (HK), phosphorylase, phosphofructokinase (PFK), glycerol-3-phosphate dehydrogenase (G-3-PDH) and lactate dehydrogenase (LDH) was carried out in the homologous leg muscles of two aquatic Birds. It appears that the leg muscle fibres of the coot, a surface swimmer are more oxidative in nature and appear to utilize glucose as source of energy. The leg muscles of the dabchick, a diving Bird, on the other hand, seem to depend on glycogen as source of energy. The relative activity levels of HK, phosphorylase and PFK support the accepted r?le of glycogen as primary substrate of carbohydrate catabolism in the leg muscles. The ratio of G-3-PDH/LDH in the leg muscles revealed that glycerol 3-phosphate cycle appears to be insufficient to account for the major part of NADH oxidation. However, the LDH activity is quite high in all the muscles. These results led us to believe that glycerol 3-phosphate cycle may function during rest, when the rate of glycolysis will be low.     

Changes in fructosediphosphate aldolase and glucose-6-phosphate dehydrogenase activity after irradiation of animals with an absolute lethal dose of gamma rays

A single total-body exposure of rats to gamma-rays in an absolutely lethal dose caused significant changes in the activity of fructosodiphosphate aldolase (ALD) and glucose-6-phosphate dehydrogenase (G-6-PDH) in the brain, liver, myocardium and skeletal muscles. The activity of ALD was mainly inhibited and that of G-6-PDH increased. Thus, the initial step of glycolysis was significantly inhibited and the key reaction of the pentose phosphate pathway enhanced in the irradiated body.     

Glucose-6-phosphate dehydrogenase plays a pivotal role in nitric oxide-involved defense against oxidative stress under salt stress in red kidney bean roots

The pivotal role of glucose-6-phosphate dehydrogenase (G-6-PDH)-mediated nitric oxide (NO) production in the tolerance to oxidative stress induced by 100 mM NaCl in red kidney bean (Phaseolus vulgaris) roots was investigated. The results show that the G-6-PDH activity was enhanced rapidly in the presence of NaCl and reached a maximum at 100 mM. Western blot analysis indicated that the increase of G-6-PDH activity in the red kidney bean roots under 100 mM NaCl was mainly due to the increased content of the G-6-PDH protein. NO production and nitrate reductase (NR) activity were also induced by 100 mM NaCl. The NO production was reduced by NaN(3) (an NR inhibitor), but not affected by N(omega)-nitro-L-arginine (L-NNA) (an NOS inhibitor). Application of 2.5 mM Na(3)PO(4), an inhibitor of G-6-PDH, blocked the increase of G-6-PDH and NR activity, as well as NO production in red kidney bean roots under 100 mM NaCl. The activities of antioxidant enzymes in red kidney bean roots increased in the presence of 100 mM NaCl or sodium nitroprusside (SNP), an NO donor. The increased activities of all antioxidant enzymes tested at 100 mM NaCl were completely inhibited by 2.5 mM Na(3)PO(4). Based on these results, we conclude that G-6-PDH plays a pivotal role in NR-dependent NO production, and in establishing tolerance of red kidney bean roots to salt stress.     

人参皂甙Rb1,Rg1,Re和Rh1对细胞脱氢酶活性的影响

应用显微分光光度术,定量地分析了人参皂甙Rb_1、Rg_1、Re、Rh_1对人胚肺成纤维细胞(2BS)和HeLa细胞脱氢酶活性的影响。结果表明,4种单体皂甙增加了高代龄2BS细胞内乳酸脱氢酶(LDH),琥珀酸脱氢酶(SDH),葡萄糖-6-磷酸脱氢酶(G-6-PDH)和丙酮酸脱氢酶(PVO)的活性,降低了HeLa细胞内这几种酶的活性。     

Activity of energy metabolism related enzymes in the myocardium and liver following administration of large doses of noradrenaline]

The activity of the glycolytic enzymes and of the glucose-6-phosphate dehydrogenase (G-6-PDH) were compared with the content of noradrenaline in rat myocardium and the liver after the intraperitoneal injection of high doses of noradrenaline. It was shown that 24 hours after int noradrenaline injection which caused exhaustion of endogenous catecholamine supply, the lactate content and the activities of lactic dehydrogenase were increased in the myocardium; the activity of hexokinase and G-6-PDH in rat myocardium and the liver were also increased, whereas the glucokinase activity was decreased. In these experiments alterations of the enzyme activities were shown to be similar to the alterations in the dystrophic tissues in which the catecholamine content was sharply decreased. The role of the sympathetic nervous system and its mediators in the mechanism of the enzyme regulation of the energy metabolism in the myocardium and the liver is discussed.     

Efficacy of Citrus reticulata and Mirazid in treatment of Schistosoma mansoni

This work has been carried out to investigate the effect of Schistosoma mansoni infection on mice livers after treatment with the ethanolic extract of Citrus reticulata root or the oleo-resin extract from Myrrh of Commiphora molmol tree (Mirazid), as a new antishistosomal drug. Marker enzymes for different cell organelles were measured; succinate dehydrogenase (SDH); lactate dehydrogenase (LDH) and its isoenzymes; glucose-6-phosphatase (G-6-Pase); acid phosphatase (AP) and 5'- nucleotidase. Liver function enzymes; aspartate aminotransferase (AST); alanine aminotransferase (ALT), and alkaline phosphatase (ALP) were also estimated. Parasitological studies through ova count and worm burden will also be taken into consideration. The results showed a marked reduction in SDH, LDH, AST, and ALT enzyme activities and a significant increase in G-6-Pase, AP, 5'- nucleotidase, and ALP after S. mansoni infection. A noticeable alteration in LDH subunits were also noticed. Treatment with C. reticulata or Mirazid improved all the previous enzyme activities with a noticeable reduction in ova count and worm burden.     

NADPH-generating system: Influence on microsomal mono-oxygenase stability during incubation for the liver-microsomal assay with rat and mouse S9 fractions

Activity levels of 7-ethoxycoumarin O-deethylase (ED), aminopyrine N-demethylase (APD), p-nitroanisoleO-demethylase (p-NAD) and glucose-6-phosphate dehydrogenase (G-6-PDH) were determined in incubation mixtures for the liver-microsomal assay (LMA) at time 0 and after 1 and 2 h incubation under conditions for mutagenic assay. The experiments were performed with S9 liver fractions from mice (induced with Na-phenobarbital and β-naphthoflavone) and rats (induced with Aroclor 1254) with and without G-6-PDH in the incubation mixtures.

In the absence of G-6-PDH the activities were significantly lower at time 0 in the mouse. The pattern of stability, however, was similar for the activities, with an increase of stability after 1 and 2 h of pre-incubation (an exception for p-NAD).

Only ED activity showed a similar behaviour in the rat. No differences were present for APD and p-NAD activities at time 0 in the rat, but the enzyme stabilities were significantly decreased after 2 h of incubation (about 15% and 10% for APD and p-NAD respectively) in the absence of G-6-PDH.

At time 0, the amounts of G-6-PDH differed between mouse and rat fractions; however, during the incubations for LMA they decreased by about 57% and 53% for the two species, respectively. In addition to the above biochemical results, the presence of exogenous G-6-PDH in the incubations for the mutagenic assay, significantly increased the mitotic gene conversion and mitotic crossing-over of dimethylnitrosamine (DMN) and AR2MNFN (a nitroimidazo[2,1-b]thiazole) in the D₇ strain of Saccharomyces cerevisiae.     

Activity and androgenic control of glycolytic enzymes in the epididymis and epididymal spermatozoa of the rat.

1. Procedures were developed for the extraction and assay of glycolytic enzymes from the epididymis and epididymal spermatozoa of the rat. 2. The epididymis was separated into four segments for analysis. When rendered free of spermatozoa by efferent duct ligation, regional differences in enzyme activity were apparent. Phosphofructokinase, glycerol phosphate dehydrogenase and glucose 6-phosphate dehydrogenase were more active in the proximal regions of the epididymis, whereas hexokinase, lactate dehydrogenase and phosphorylase were more active in the distal segment. These enzymes were less active in the epididymis of castrated animals and less difference was apparent between the proximal and distal segments. However, the corpus epididymidis from castrated rats had lower activities of almost all enzymes compared with other epididymal segments. 3. Spermatozoa required sonication to obtain satisfactory enzyme release. Glycolytic enzymes were more active in spermatozoa than in epididymal tissue, being more than 10 times as active in the case of hexokinase, phosphoglycerate kinase and phosphoglycerate mutase. 4. The specific activities of a number of enzymes in the epididymis were dependent on the androgen status of the animal. These included hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase, glycerol phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphorylase. 5. The caput and cauda epididymidis differed in the extent to which enzyme activities changed in response to an altered androgen status. The most notable examples were hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, 6-phosphogluconate dehydrogenase and phosphorylase.