scholarly journals Genome-Wide Identification of Mango (Mangifera indica L.) Polygalacturonases: Expression Analysis of Family Members and Total Enzyme Activity During Fruit Ripening

2019 ◽  
Vol 10 ◽  
Author(s):  
Mitzuko Dautt-Castro ◽  
Andrés G. López-Virgen ◽  
Adrian Ochoa-Leyva ◽  
Carmen A. Contreras-Vergara ◽  
Ana P. Sortillón-Sortillón ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Expression Analysis ◽  
Fruit Ripening ◽  
Mangifera Indica ◽  
Family Members ◽  
Total Enzyme Activity ◽  
Genome Wide ◽  
Total Enzyme

scholarly journals Two-Step Production of Neofructo-Oligosaccharides Using Immobilized Heterologous Aspergillus terreus 1F-Fructosyltransferase Expressed in Kluyveromyces lactis and Native Xanthophyllomyces dendrorhous G6-Fructosyltransferase

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 673 ◽  
Author(s):  
Burghardt ◽  
Baas ◽  
Gerlach ◽  
Czermak
Keyword(s):  
Response Surface Methodology ◽  
Enzyme Activity ◽  
Reaction Time ◽  
Aspergillus Terreus ◽  
Kluyveromyces Lactis ◽  
Xanthophyllomyces Dendrorhous ◽  
Initial Concentration ◽  
Total Enzyme Activity ◽  
Glycosidic Bonds ◽  
Total Enzyme

Fructo-oligosaccharides (FOS) are prebiotic low-calorie sweeteners that are synthesized by the transfer of fructose units from sucrose by enzymes known as fructosyltransferases. If these enzymes generate β-(2,6) glycosidic bonds, the resulting oligosaccharides belong to the neoseries (neoFOS). Here, we characterized the properties of three different fructosyltransferases using a design of experiments approach based on response surface methodology with a D-optimal design. The reaction time, pH, temperature, and substrate concentration were used as parameters to predict three responses: The total enzyme activity, the concentration of neoFOS and the neoFOS yield relative to the initial concentration of sucrose. We also conducted immobilization studies to establish a cascade reaction for neoFOS production with two different fructosyltransferases, achieving a total FOS yield of 47.02 ± 3.02%. The resulting FOS mixture included 53.07 ± 1.66 mM neonystose (neo-GF3) and 20.8 ± 1.91 mM neo-GF4.

scholarly journals The effects of starvation and experimental diabetes on phosphoenol-pyruvate carboxykinase in the guinea pig

1977 ◽  
Vol 164 (2) ◽  
pp. 357-361 ◽  
Author(s):  
K R F Elliott ◽  
C I Pogson
Keyword(s):  
Enzyme Activity ◽  
Guinea Pig ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Blood Glucose Concentration ◽  
Mitochondrial Fraction ◽  
Kidney Cortex ◽  
Total Enzyme Activity ◽  
The Mean ◽  
Mean Blood Glucose ◽  
Total Enzyme

1. Approx. 85% of liver phosphoenolpyruvate carboxykinase is associated with the mitochondrial fraction in the fed guinea pig. Enzyme activity is unchanged in diabetes, but doubles during starvation. In contrast with earlier reports, both cytoplasmic and mitochondrial activities were found to be increased. 2. In kidney cortex, total enzyme activity is increased in both starved and diabetic animals. These changes are associated with increases in the cytoplasmic activity alone. 3. In diabetic animals the mean blood-glucose concentration was 23.1 mM. Other blood metabolites were lower than those in the rat, and the animals did not show significant ketosis. 4. Changes in the rates of gluconeogenesis from lactate and propionate paralleled those in phosphoenolpyruvate carboxykinase activity.

Changes in mass and catalytic activity concentrations of aspartate aminotransferase isoenzymes in serum after a myocardial infarction.

1986 ◽  
Vol 32 (3) ◽  
pp. 496-500 ◽  
Author(s):  
A E Niblock ◽  
G Jablonsky ◽  
F Y Leung ◽  
A R Henderson
Keyword(s):  
Myocardial Infarction ◽  
Enzyme Activity ◽  
Catalytic Activity ◽  
Aspartate Aminotransferase ◽  
Left Ventricular ◽  
Peak Activity ◽  
Ventricular Failure ◽  
Total Enzyme Activity ◽  
Activity Concentrations ◽  
Total Enzyme

Abstract We used an RIA and inhibition of enzyme activity to monitor the changes in mass and catalytic concentrations of the aspartate aminotransferase (EC 2.6.1.1;AST) isoenzymes in serum after myocardial infarction. Cytosolic (c-AST) and mitochondrial (m-AST) forms of AST were present in sera from all 38 of our patients. Although the immunological and catalytic concentrations of both isoenzymes correlated well with the size of the infarct, c-AST gave a better measure than did m-AST. About 20% of the total enzyme activity at peak activity was from the mitochondrial isoenzyme. Both isoenzyme activities peak at very nearly the same time, but m-AST has the longer half-life. Immunological evidence of the mitochondrial isoenzyme can be detected in serum for at least eight days after the infarct. The presence of left ventricular failure produces greater serum isoenzyme activities than in those without failure.

scholarly journals The effect of thiamin on the activation of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in Euglena gracilis

1993 ◽  
Vol 292 (2) ◽  
pp. 463-467 ◽  
Author(s):  
S Shigeoka ◽  
Y Nakano
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Euglena Gracilis ◽  
Total Activity ◽  
Immunoblot Analysis ◽  
Decarboxylase Activity ◽  
Total Enzyme Activity ◽  
Thiamin Pyrophosphate ◽  
Total Enzyme

The effect of thiamin on thiamin pyrophosphate-dependent 2-oxoglutarate (2-OG) decarboxylase activity in Euglena gracilis was investigated. The total activity of 2-OG decarboxylase in thiamin-sufficient cells in 3 times that in thiamin-deficient cells. The addition of thiamin to thiamin-deficient cells causes the total enzyme and holoenzyme activities to increase and reach similar levels to that in thiamin-sufficient cells. Cycloheximide and chloramphenicol, inhibitors of protein synthesis, have no effect on the total enzyme activity. Immunochemical titration and determination of 2-OG decarboxylase mRNA by using an antibody directed against Euglena 2-OG decarboxylase indicate that the increase in the holoenzyme activity of 2-OG decarboxylase is due to activation of pre-existing protein and does not require synthesis of new proteins in thiamin-deficient cells. During the period of the increase in the total activity, the apoenzyme increases and reaches a temporary peak in 2 h. Immunoblot analysis demonstrates that the precursor form (a 65 kDa subunit) of 2-OG decarboxylase in thiamin-deficient cells is more abundant than that in thiamin-sufficient cells and the increase in the apoenzyme by addition of thiamin results from the conversion of the precursor form into the mature form (a 62 kDa subunit).

Effects of pyridostingmine on acetylcholinesterase in different muscles of the mouse

1997 ◽  
Vol 16 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Maxine C Lintern ◽  
Margaret E Smith ◽  
C Brian Ferry
Keyword(s):  
Enzyme Activity ◽  
Extensor Digitorum Longus ◽  
Low Dose ◽  
Control Level ◽  
Extensor Digitorum ◽  
Molecular Forms ◽  
High Dose ◽  
Total Enzyme Activity ◽  
Delayed Effects ◽  
Total Enzyme

1 Pyridostigmine bromide was administered subcuta neously in mice, in a dose of 0.4 or 2.0 ?moles/kg, and the activity of the predominant (G1, G4, and A12) molecular forms of acetylcholinesterase were exam ined in diaphragm, extensor digitorum longus (EDL), and soleus muscles at 3 h, 6 h, 24 h and 5 days. 2 In diaphragm, no effect was apparent after the low dose, but after the high dose there was a reduction in activity of the functional A12 form at 24 h, followed by an increase which had overshot the control level at 5 days. 3 In the fast EDL, after the low dose, all three molecular forms were decreased at 3 h, but had returned to normal by 6 h. This effect was not apparent after the high dose. 4 In the slow soleus the low dose caused a significant increase in total enzyme activity at 5 days, but the high dose caused significant increases in all molecular forms at 3 hours. 5 Thus pyridostigmine had delayed effects on the levels of acetylcholinesterase. The three muscles displayed different sensitivities to the drug, but the changes were consistent with initial inhibition of the activity leading to down-regulation of the enzyme followed by up- regulation, which could overshoot the normal levels.

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