scholarly journals Novel coronavirus vulnerability: metabolic derangements and altered dehydrogenase enzyme activities are central to the virus pathogenesis in human, bat and other animals

2021 ◽  
Vol 11 (1) ◽  
pp. 1
Author(s):  
Sanjib Kumar Manna
Keyword(s):  
Enzyme Activities ◽  
Dehydrogenase Enzyme ◽  
Novel Coronavirus

Evaluation of state and evolution of marine fish waste composting by enzyme activities

2017 ◽  
Vol 44 (5) ◽  
pp. 348-357 ◽  
Author(s):  
Khoshrooz Kazemi ◽  
Baiyu Zhang ◽  
Leonard M. Lye ◽  
Zhiwen Zhu
Keyword(s):  
Marine Fish ◽  
Enzyme Activities ◽  
The State ◽  
Fish Waste ◽  
Composting Process ◽  
Physiochemical Parameters ◽  
Dehydrogenase Enzyme ◽  
Carbon Nitrogen Ratio ◽  
Nitrogen Ratio ◽  
Mature Fish

The feasibility of using enzyme activities for indicating the state of marine fish waste composting was examined in this study and the evolution of the composting process for a 60 day period was evaluated. Results indicated that stable and mature fish waste compost has been generated. During the composting process, oxidoreductase enzyme (dehydrogenase) and hydrolase enzyme (β-glucosidase and phosphatase) activities decreased with time since available organic compounds decreased. A good correlation among enzyme activities and different physiochemical parameters including oxygen uptake rate, carbon/nitrogen ratio, and germination index led to the conclusion that both hydrolytic and dehydrogenase enzyme activities could be feasible indicators of the state and evolution of the composting process.

Human glyceraldehyde-3-phosphate dehydrogenase: mRNA levels and enzyme activity in developing muscle

1985 ◽  
Vol 5 (8) ◽  
pp. 2147-2149
Author(s):  
Y H Edwards ◽  
J C Lloyd ◽  
S L McMillan ◽  
F J Benham
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Cardiac Muscle ◽  
Enzyme Activities ◽  
Mrna Levels ◽  
Adult Tissue ◽  
Adult Skeletal Muscle ◽  
Polyadenylated Rna ◽  
Dehydrogenase Enzyme ◽  
Developing Muscle

Analysis of human glyceraldehyde-3-phosphate dehydrogenase mRNA revealed that levels in adult skeletal muscle are 12-fold greater per microgram of polyadenylated RNA than in fetal skeletal muscle, whereas in cardiac muscle RNA levels were about equal in fetal and adult tissue. The mRNA levels correlate well with glyceraldehyde 3-phosphate dehydrogenase enzyme activities. There was no evidence for fetus- or tissue-specific forms.

scholarly journals Human glyceraldehyde-3-phosphate dehydrogenase: mRNA levels and enzyme activity in developing muscle.

1985 ◽  
Vol 5 (8) ◽  
pp. 2147-2149 ◽  
Author(s):  
Y H Edwards ◽  
J C Lloyd ◽  
S L McMillan ◽  
F J Benham
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Cardiac Muscle ◽  
Enzyme Activities ◽  
Mrna Levels ◽  
Adult Tissue ◽  
Adult Skeletal Muscle ◽  
Polyadenylated Rna ◽  
Dehydrogenase Enzyme ◽  
Developing Muscle

Analysis of human glyceraldehyde-3-phosphate dehydrogenase mRNA revealed that levels in adult skeletal muscle are 12-fold greater per microgram of polyadenylated RNA than in fetal skeletal muscle, whereas in cardiac muscle RNA levels were about equal in fetal and adult tissue. The mRNA levels correlate well with glyceraldehyde 3-phosphate dehydrogenase enzyme activities. There was no evidence for fetus- or tissue-specific forms.

High time resolution enzyme cytochemistry of rod outer segment

1990 ◽  
Vol 48 (3) ◽  
pp. 878-879
Author(s):  
Takuma Saito ◽  
Toshihiro Takizawa
Keyword(s):  
Enzyme Activities ◽  
Outer Segment ◽  
Rapid Change ◽  
High Time Resolution ◽  
Visual Cell ◽  
Enzyme Cytochemistry ◽  
Activation Effect ◽  
Rod Outer Segment ◽  
Enzymatic Cascades ◽  
Rapid Drop

Cells and tissues live on a number of dynamic metabolic pathways, which are made up of sequential enzymatic cascades.Recent biochemical and physiological studies of vision research showed the importance of cGMP metabolism in the rod outer segment of visual cell, indicat ing that the photon activated rhodopsin exerts activation effect on the GTP binding protein, transducin, and this act ivated transducin further activates phosphodiesterase (PDEase) to result in a rapid drop in cGMP concentration in the cytoplasm of rod outer segment. This rapid drop of cGMP concentration exerts to close the ion channel on the plasma membrane and to stop of inward current brings hyperpolarization and evokes an action potential.These sequential change of enzyme activities, known as cGMP cascade, proceeds quite rapidly within msec order. Such a rapid change of enzyme activities, such as PDEase in rod outer segment, was not a matter of conventional histochemical invest igations.

Tryptophan-Niacin Metabolism in Rat with Puromycin Aminonucleoside-Induced Nephrosis

2006 ◽  
Vol 76 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Yukari Egashira ◽  
Shin Nagaki ◽  
Hiroo Sanada
Keyword(s):  
Body Weight ◽  
Urinary Excretion ◽  
Enzyme Activities ◽  
Treated Group ◽  
Control Group ◽  
Puromycin Aminonucleoside ◽  
Low Level ◽  
Key Enzyme

We investigated the change of tryptophan-niacin metabolism in rats with puromycin aminonucleoside PAN-induced nephrosis, the mechanisms responsible for their change of urinary excretion of nicotinamide and its metabolites, and the role of the kidney in tryptophan-niacin conversion. PAN-treated rats were intraperitoneally injected once with a 1.0% (w/v) solution of PAN at a dose of 100 mg/kg body weight. The collection of 24-hour urine was conducted 8 days after PAN injection. Daily urinary excretion of nicotinamide and its metabolites, liver and blood NAD, and key enzyme activities of tryptophan-niacin metabolism were determined. In PAN-treated rats, the sum of urinary excretion of nicotinamide and its metabolites was significantly lower compared with controls. The kidneyα-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) activity in the PAN-treated group was significantly decreased by 50%, compared with the control group. Although kidney ACMSD activity was reduced, the conversion of tryptophan to niacin tended to be lower in the PAN-treated rats. A decrease in urinary excretion of niacin and the conversion of tryptophan to niacin in nephrotic rats may contribute to a low level of blood tryptophan. The role of kidney ACMSD activity may be minimal concerning tryptophan-niacin conversion under this experimental condition.

Sign in / Sign up

Export Citation Format

Share Document