Effect of native and modified starches on nutritional and physiological performance of wild juveniles of red grouper (Epinephelus morio)

The aim of this study was to evaluate carbohydratesutilization by wild red grouper Epinephelus morio.Juveniles were fed during 93 d on a selection of starches: native raw cornstarch (RCS), waxy cornstarch (WCS), raw potato starch (RPS) and gelatinized potato starch (GP) at 20% inclusion level. The best growth was obtained in fish fed cornstarch either native raw of waxy cornstarch (p<0.05). Hepatosomatic index and blood glucose (40 mg dL-1) were similar as well as hematocrit values (50%) (p>0.05), whereas glycogen content increased up to 200 mg g-1with waxy cornstarch. Specific activity of a-glucosidase and α-amylase remained stable (p>0.05). Hepatic glycolytic enzymes increased with raw native and waxy cornstarch (p<0.05); metabolic enzyme glucose 6 phosphate dehydrogenase (G6P-DH) was activated with raw native cornstarch (p<0.05) while pyruvate kinase (PK) remained stable regardless of treatments (p>0.05). Hexokinase (HK1) and glucokinase (GK) varied according to carbohydrate source: values were higher with cornstarches than potato starches (p<0.05). Pentose monophosphate shunt (HMS) remained not altered by starch sources (p>0.05). In final, the low size of granules from cornstarch favored the assimilation in liver of wild juveniles red grouper.

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Development of metabolic enzyme activity in locomotor and cardiac muscles of the migratory barnacle goose

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1995.269.1.r64 ◽

1995 ◽

Vol 269 (1) ◽

pp. R64-R72 ◽

Cited By ~ 14

Author(s):

C. M. Bishop ◽

P. J. Butler ◽

S. Egginton ◽

A. J. el Haj ◽

G. W. Gabrielsen

Keyword(s):

Plasma Glucose ◽

Citrate Synthase ◽

Specific Activity ◽

Glycolytic Enzymes ◽

Metabolic Enzyme ◽

Mitochondrial Enzymes ◽

Pectoralis Muscle ◽

Barnacle Goose ◽

Average Maximum ◽

Cardiac Muscles

Preflight development of the goslings was typified by rapid increases in the mitochondrial enzymes of the semimembranosus and heart ventricular muscles resulting in near-adult values by 3 wk of age. In contrast, aerobic capacity of the pectoralis muscle initially developed slowly but showed a rapid increase between 5 and 7 wk of age, in preparation for becoming airborne. Activities of glycolytic enzymes in the pectoralis muscle showed similar patterns of development as those found for the aerobic enzymes, except for hexokinase, which was low at all ages, indicating an adaptation for catabolism of both intracellular glycogen and plasma fatty acids in preference to plasma glucose. Muscle mass specific activity of citrate synthase in the pectoralis increased by only 33% from goslings during the first few days of flight, compared with premigratory geese. Activities of anaerobic glycolytic enzymes in the ventricles were low, but values for hexokinase, which is involved in the phosphorylation of plasma glucose, developed rapidly. Values for lactate dehydrogenase were also high, reflecting the capacity of the heart to catabolize plasma lactate. Substrate flux supplied by carnitine palmitoyltransferase and oxoglutarate dehydrogenase (OGD), in the pectoralis muscles of the premigratory geese, appears to have the smallest excess capacities to meet the requirements of sustained aerobic flight. The average maximum oxygen uptake for premigratory geese during flight, as indicated by values for OGD, is calculated to be 484 ml O2/min (or 208 ml O2.min-1.kg-1).

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Properties of High-Swelling Native Starch Treated by Heat–Moisture Treatment with Different Holding Times and Iterations

Molecules ◽

10.3390/molecules25235528 ◽

2020 ◽

Vol 25 (23) ◽

pp. 5528

Author(s):

Chia-Long Lin ◽

Jheng-Hua Lin ◽

Jia-Jing Lin ◽

Yung-Ho Chang

Keyword(s):

Potato Starch ◽

Pasting Properties ◽

Degree Of Polymerization ◽

Viscosity Change ◽

Tapioca Starch ◽

Heat Moisture Treatment ◽

Moisture Treatment ◽

Severe-glucose-6-phosphate dehydrogenase (G6PD) deficiency associated with chronic hemolytic anemia, granulocyte dysfunction, and increased susceptibility to infections: description of a new molecular variant (G6PD Barcelona)

Blood ◽

10.1182/blood.v59.2.428.428 ◽

1982 ◽

Vol 59 (2) ◽

pp. 428-434 ◽

Cited By ~ 41

Author(s):

JL Vives Corrons ◽

E Feliu ◽

MA Pujades ◽

F Cardellach ◽

C Rozman ◽

...

Keyword(s):

Hemolytic Anemia ◽

G6pd Deficiency ◽

Specific Activity ◽

Heat Stability ◽

Molecular Characteristics ◽

Functional Studies ◽

Leukocyte Alkaline Phosphatase ◽

Severe Deficiency ◽

Glucose 6 Phosphate Dehydrogenase ◽

Increased Susceptibility

Abstract Molecular, kinetic, and functional studies were carried out on erythrocytes and leukocytes in a Spanish male with G6PD deficiency, congenital nonspherocytic hemolytic anemia (CNSHA), and increased susceptibility to infections. G6PD activity was absent in patient's red cells and was about 2% of normal in leukocytes. Molecular studies using standard methods (WHO, 1967) showed G6PD in the patient to have a slightly fast electrophoretic mobility at pH 8.0 with otherwise normal properties (heat stability at 46 degrees C, apparent affinity for substrates, optimum pH, and utilization of substrate analogues). Other tests showed the patient's granulocytes to engulf latex particles normally, but to have impaired reduction of nitroblue tetrazolium and ferricytochrome-c as well as reduced iodination. Chemotaxis and random migration of the patient's granulocytes were normal as were myeloperoxidase, leukocyte alkaline phosphatase (LAP), and ultrastructural features. The molecular characteristics of G6PD in the patient differed from those of all previously reported variants associated with CNSHA, so the present variant was provisionally called G6PD Barcelona to distinguish it from other G6PD variants previously described. Possible mechanisms for the severe deficiency of G6PD in erythrocytes and granulocytes was investigated by studies on the immunologic specific activity of the mutant enzyme.

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Low dietary inclusion of nutraceuticals from microalgae improves feed efficiency and modifies intermediary metabolisms in gilthead sea bream (Sparus aurata)

Scientific Reports ◽

10.1038/s41598-020-75693-3 ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

Erick Perera ◽

David Sánchez-Ruiz ◽

María Isabel Sáez ◽

Alba Galafat ◽

André Barany ◽

...

Keyword(s):

Feed Efficiency ◽

Sparus Aurata ◽

Control Diet ◽

Sea Bream ◽

Metabolic Enzyme ◽

Hepatosomatic Index ◽

Hepatic Glycogen ◽

Gilthead Seabream ◽

Plasma Lactate ◽

Alpha Linolenic Acid

Abstract The aim of this work was to evaluate two functional feeds for the gilthead seabream, Sparus aurata, containing low inclusion of two microalgae-based products (LB-GREENboost, LBGb; and LB-GUThealth, LBGh). Fish (12–13 g) were fed for 13 weeks a control diet or one of the four diets supplemented with both products at 0.5% or 1%. LBGb and LBGh did not affect specific growth rate or survival, but increased feed efficiency by decreasing feed intake and enlarging the intestines. LBGb increased hepatosomatic index and reduced cortisol levels in plasma, while both products lowered plasma lactate. Extensive metabolite and metabolic enzyme profiling revealed that microalgae supplementations, especially 1% LBGh: (i) decrease plasma lactate and increase hepatic glycogen, (ii) reduce hepatic gluconeogenesis, (iii) enhance hepatic lipogenic activity and lipid secretion, (iv) led fish to double triglyceride content in muscle and to stimulate its lipid oxidative capacity, and (v) increase the content of monounsaturated fatty acids and the omega-3 alpha-linolenic acid in muscle. This study demonstrates that both microalgae-based products are suited to improve feed efficiency and orchestrate significant changes in the intermediary metabolism in gilthead seabream juveniles.

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Enhanced expression of glucose-6-phosphate dehydrogenase in human cells sustaining oxidative stress

Biochemical Journal ◽

10.1042/bj3230801 ◽

1997 ◽

Vol 323 (3) ◽

pp. 801-806 ◽

Cited By ~ 114

Author(s):

Matilde V. URSINI ◽

Angelina PARRELLA ◽

Graziella ROSA ◽

Salvatore SALZANO ◽

Giuseppe MARTINI

Keyword(s):

Oxidative Stress ◽

Mammalian Cells ◽

Specific Activity ◽

Redox Status ◽

Enzyme Synthesis ◽

Oxygen Intermediates ◽

New Information ◽

Enhanced Expression ◽

A Minor ◽

Glucose 6 Phosphate Dehydrogenase

Recent reports have demonstrated that glucose-6-phosphate dehydrogenase (G6PD) activity in mammalian cells is necessary in order to ensure cell survival when damage is produced by reactive oxygen intermediates. In this paper we demonstrate that oxidative stress, caused by agents acting at different steps in the biochemical pathway controlling the intracellular redox status, determines the increase in G6PD-specific activity in human cell lines of different tissue origins. The intracellular level of G6PD-specific mRNA also increases, with kinetics compatible with the induction of new enzyme synthesis. We carried out experiments in which cells were exposed to oxidative stress in the presence of inhibitors of protein or RNA synthesis. These demonstrated that increased G6PD expression is mainly due to an increased rate of transcription, with a minor but significant contribution of regulatory mechanisms acting at post-transcriptional levels. These results provide new information on the defence systems that eukaryotic cells possess in order to prevent damage caused by potentially harmful oxygen derivatives.

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Expression of metabolic enzyme genes and heat-shock protein genes during embryonic development in diapause and non-diapause egg of multivoltine silkworm Bombyx mori

Biologia ◽

10.2478/s11756-008-0124-x ◽

2008 ◽

Vol 63 (5) ◽

Cited By ~ 12

Author(s):

Ragunathan Saravanakumar ◽

Kangayam Ponnuvel ◽

Syed Qadri

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Bombyx Mori ◽

Early Stage ◽

Metabolic Enzyme ◽

Dehydrogenase Gene ◽

Heat Shock Protein Genes ◽

High Level ◽

Glucose 6 Phosphate Dehydrogenase ◽

Silkworm Bombyx Mori

AbstractThe expression of metabolic enzyme genes and heat-shock protein genes (Hsp) during early embryogenesis in diapause and non-diapause eggs of the silkworm Bombyx mori was quantified by semi-quantitative RT-PCR. The trehalase gene (Tre) was expressed in non-diapause eggs up-to nine days, while in diapause eggs was not up regulated. The glycogen phosphorylase gene (GPase) was expressed in non-diapause eggs, whereas in diapause eggs a high level was observed in early stage, but down regulated in later stage. The phosphofructokinase gene (PFK) and sorbitol dehyrogenase-2 gene (SDH-2) expression was fluctuated in non-diapause eggs, whereas in diapause eggs these were expressed only at early stage and not observed in later stage. The glucose-6-phosphate dehydrogenase gene (G6P-DH) in non-diapause eggs was highly expressed during the differentiation phase and decreased in the organogenesis phase. In contrast to this, expression in diapause eggs was of low level during differentiation phase and of high level observed in the organogenesis phase. In the tissues, PFK and SDH-2 were selectively expressed in cuticle and midgut, whereas Tre expression was high in midgut and ovary of larvae incubated at 15°C. The Hsp (20.4, 20.8, 40, 70, and 90) were expressed in both diapause and non-diapause eggs. Their expression was, however, selective in tissues with Hsp20.4 in midgut and ovary, Hsp40 in head, Hsp70 in cuticle and Hsp90 in ovary and head in high amounts at 15°C. These results suggest that the metabolic enzyme genes studied except Hsp play a major role during embryogenesis of diapause and non-diapause silkworm.

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Effects of aldosterone on blood pressure and glucose-6-phosphate dehydrogenase activity of heart muscle

Canadian Journal of Physiology and Pharmacology ◽

10.1139/y69-033 ◽

1969 ◽

Vol 47 (2) ◽

pp. 193-197 ◽

Cited By ~ 4

Author(s):

C. C. Liew ◽

A. G. Gornall

Keyword(s):

Blood Pressure ◽

Body Weight ◽

Heart Muscle ◽

Specific Activity ◽

Systolic Pressure ◽

Experimental Hypertension ◽

Low Doses ◽

Significant Elevation ◽

Desoxycorticosterone Acetate ◽

Glucose 6 Phosphate Dehydrogenase

A study was made of the effects of aldosterone on the activity of heart muscle glucose-6-phosphate dehydrogenase (G6PDH) in relation to the pathogenesis of experimental hypertension. In a 17-day experiment, with rats given daily 1-μg doses of aldosterone/100 g body weight, no change in systolic pressure occurred and the specific activity (s.a.) of heart muscle G6PDH declined. Rats receiving daily 100 μg of aldosterone, or 500 μg of desoxycorticosterone acetate (DOCA) per 100 g body weight, showed a significant elevation of systolic pressure by the 17th day. This effect was accompanied by increases in the s.a. of heart muscle G6PDH, apparently preceding the development of hypertension. Evidence for a homeostatic role for aldosterone was revealed by the ability of low doses to prevent a decline in s.a. of cardiac G6PDH during fasting, and to reverse the increase produced by DOCA.

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PRODUCTION OF SYRUPS FROM WHEAT, POTATO, TAPIOCA, AND WAXY CEREAL STARCHES

Canadian Journal of Research ◽

10.1139/cjr48f-029 ◽

1948 ◽

Vol 26f (7) ◽

pp. 284-296 ◽

Cited By ~ 2

Author(s):

K. A. Clendenning ◽

D. E. Wright

Keyword(s):

Tap Water ◽

Potato Starch ◽

Filter Press ◽

Hydrolysis Rate ◽

Sodium Bisulphite ◽

Low Protein ◽

Color Development ◽

Plant Equipment ◽

Waxy Corn ◽

Potato Starches

Syrups prepared in semipilot plant equipment from wheat, corn, waxy corn, tapioca, and potato starches of low protein content were almost identical in taste and appearance. Differences in nature and amount of non-carbohydrate constituents did not necessitate modifications of the process. Wheat, corn, and waxy corn slurries hydrolyzed at approximately the same rate with 0.2% hydrochloric acid whereas potato starch hydrolyzed less rapidly. Contamination with 1.6% protein did not depress the hydrolysis rate but promoted foaming, turbidity, and bitterness. Loss of insoluble solids on the filter press averaged 1.25% for cereal and 0.3% for potato starch hydrolyzates. Complete decolorization of 14° and 30° Bé. syrup was effected by 0.5% activated carbon, based on the juice weight at each stage. Tap water promoted color development in the evaporator and inhibited color removal by active carbon. Color and fluorescence development in stored syrups was promoted by protein impurities, light, and tap water, and was strongly inhibited by sodium bisulphite. Syrups that remained colorless almost indefinitely were prepared from prime quality starches by using distilled water in the process and either acid-extracted carbon or bone char as decolorizing agents.

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Effects of some antibiotics on glucose 6-phosphate dehydrogenase in sheep liver

Veterinární Medicína ◽

10.17221/5836-vetmed ◽

2012 ◽

Vol 47 (No. 10 - 11) ◽

pp. 283-288 ◽

Cited By ~ 4

Author(s):

M. Çiftci ◽

V. Turkoglu ◽

S. Aldemir

Keyword(s):

Gel Electrophoresis ◽

Enzyme Purification ◽

Specific Activity ◽

Polyacrylamide Gel Electrophoresis ◽

Sheep Liver ◽

Sds Page ◽

In Vitro Effects ◽

Glucose 6 Phosphate Dehydrogenase ◽

Sepharose 4B

In vitro effects of penicillin, sulbactam, cefazolin, and amikacine on the activity of the enzyme glucose-6-phosphate dehydrogenase in sheep liver were investigated. Glucose 6-phosphate dehydrogenase was purified from sheep liver, using a simple and rapid method. The purification consisted of two steps, preparation of homogenate and 2’, 5’-ADP Sepharose 4B affinity chromatography. As a result of the two consecutive procedures, the enzyme, having the specific activity of 11.76 EU/mg proteins, was purified with a yield of 35.72% and 1.913 fold. In order to control the enzyme purification SDS polyacrylamide gel electrophoresis (SDS-PAGE) was done. SDS-PAGE showed a single band for the enzyme. In addition, I50 values of the antibiotics were determined by plotting activity % vs. antibiotic concentrations. I50 values were 17.71 mM for penicillin, 27.38 mM for sulbactam, 28.88 mM for cefazolin, and 30.59 mM for amikacine.

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Glucose-6-phosphate dehydrogenase increases Ca2+ currents by interacting with Cav1.2 and reducing intrinsic inactivation of the L-type calcium channel

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.00727.2019 ◽

2020 ◽

Vol 319 (1) ◽

pp. H144-H158 ◽

Cited By ~ 1

Author(s):

Rakhee Gupte ◽

Vidhi Dhagia ◽

Petra Rocic ◽

Rikuo Ochi ◽

Sachin A. Gupte

Keyword(s):

Blood Pressure ◽

Metabolic Syndrome ◽

Smooth Muscle ◽

Calcium Channel ◽

Smooth Muscle Cell ◽

Crucial Role ◽

Vascular Function ◽

Metabolic Enzyme ◽

Glucose 6 Phosphate Dehydrogenase ◽

Expression And Activity

In this study we have identified a novel isozyme of glucose-6-phosphate dehydrogenase (G6PD), a metabolic enzyme, that interacts with and contributes to regulate smooth muscle cell L-type Ca2+ ion channel function, which plays a crucial role in vascular function in physiology and pathophysiology. Furthermore, we demonstrate that expression and activity of this novel G6PD isoform are increased in arteries of individuals with metabolic syndrome and in inhibition of G6PD activity in rats of metabolic syndrome reduced blood pressure.

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