A bifunctional protein with deficient enzymic activity: Identification of a new peroxisomal disorder using novel methods to measure the peroxisomal β-oxidation enzyme activities

1990 ◽  
Vol 13 (3) ◽  
pp. 375-379 ◽  
Author(s):  
R. J. A. Wanders ◽  
C. W. T. van Roermund ◽  
A. Schelen ◽  
R. B. H. Schutgens ◽  
J. M. Tager ◽  
...  
Keyword(s):  
Enzyme Activities ◽  
Enzymic Activity ◽  
Peroxisomal Disorder ◽  
Bifunctional Protein ◽  
Novel Methods ◽  
Oxidation Enzyme

The persistence and toxicity of pesticides in relation to enzymic activity

1975 ◽  
Vol 8 (4) ◽  
pp. 201-205 ◽  
Author(s):  
C H Walker
Keyword(s):  
Enzyme Activities ◽  
Enzymic Activity ◽  
Central Question ◽  
Detoxifying Enzymes ◽  
Selective Pesticides

The degree of significance of enzyme activities in determining the rate of elimination of pesticides by vertebrates and insects is a central question in the study of their toxicity. Resistance to a particular pesticide may be greater where detoxifying enzymes are more active, and may be reduced by addition of inhibitors which block such activity selectively. Knowledge of enzymic differences between species should aid development of new selective pesticides of short persistence.

scholarly journals Correlated changes of some enzyme activities and cofactor and substrate contents of pea cotyledon tissue during germination

1968 ◽  
Vol 108 (3) ◽  
pp. 437-444 ◽  
Author(s):  
A. P. Brown ◽  
J. L. Wray
Keyword(s):  
Oxidation State ◽  
Enzyme Activities ◽  
Inorganic Phosphate ◽  
Enzymic Activity ◽  
Phosphoglucose Isomerase ◽  
Nadh Ratio ◽  
Tissue Contents ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Substrate Concentrations ◽  
Specific Control

1. The activities of six enzymes (hexokinase, phosphoglucose isomerase, phosphofructokinase, aldolase, glucose 6-phosphate dehydrogenase and amylase) in extracts of pea cotyledons were determined. The activities during the first 10 days after germination showed individual and characteristic changes that indicate a specific control of both synthesis and destruction of enzymes. 2. Tissue contents of glucose, inorganic phosphate, glucose 6-phosphate, fructose 6-phosphate, ATP, ADP, AMP, NAD and NADP were also determined, and a correlation is reported between the substrate concentrations at day 1 and the subsequent enzymic activity. 3. The initial NAD+/NADH ratio value of 1 changed to about 3 by day 4; the NADP content was lower and changes in the oxidation state were less striking. The ratio of ATP to ADP and AMP remained virtually constant.

scholarly journals d-3-Hydroxyacyl-CoA Dehydratase/d-3-Hydroxyacyl-CoA Dehydrogenase Bifunctional Protein Deficiency: A Newly Identified Peroxisomal Disorder

1997 ◽  
Vol 61 (5) ◽  
pp. 1153-1162 ◽  
Author(s):  
Yasuyuki Suzuki ◽  
Ling Ling Jiang ◽  
Masayoshi Souri ◽  
Shoko Miyazawa ◽  
Seiji Fukuda ◽  
...  
Keyword(s):  
Peroxisomal Disorder ◽  
Protein Deficiency ◽  
Bifunctional Protein ◽  
Hydroxyacyl Coa Dehydrogenase

The secreted and somatic proteinases of the bovine lungwormDictyocaulus viviparusand their inhibition by antibody from infected and vaccinated animals

Parasitology ◽  
1992 ◽  
Vol 105 (2) ◽  
pp. 325-333 ◽  
Author(s):  
C. Britton ◽  
D. P. Knox ◽  
G. J. Canto ◽  
G.M. Urquhart ◽  
M. W. Kennedy
Keyword(s):  
Antibody Response ◽  
Enzyme Activities ◽  
Gel Electrophoresis ◽  
Enzymic Activity ◽  
Protein G ◽  
Active Principle ◽  
Igg Antibody ◽  
Substrate Specificities ◽  
Protein Substrates ◽  
Dictyocaulus Viviparus

SUMMARYProteinase activities were examined in extracts and excretory–secretory (ES) products of the infective and adult stages of the cattle lungworm,Dictyocaulus viviparus. Multiple enzyme activities were identified from each source, as defined by pH optima, substrate specificities, inhibitor effects and substrate gel electrophoresis. Serine-, cysteine- and metalloproteinases were identified, secreted materials being more active against protein substrates per unit protein than were extracts, and the particular proteinases produced varied with the developmental stage of the parasite. The antigenicity of these parasite proteinases was demonstrated by the inhibition of enzymic activity with Protein G-purified serum IgG antibody from both infected and vaccinated hosts and in the retardation of enzyme migration on electrophoresis of enzyme–antibody complexes. For the adult products, this confirmed that the enzymes concerned were of parasite origin, and not host-derived. These results argue for investigation ofD. viviparusproteinases as targets for the antibody response in the limitation of parasite-mediated tissue damage and as the active principle behind the anti-D. viviparusvaccine.

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.

Effect of a constant supply of different nitrogen sources on protein and carbohydrate content and enzyme activities of Anabaena variabilis cells

1995 ◽  
Vol 95 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Andres P Sanz ◽  
Conrado Moreno-Vivian ◽  
Jose M. Maldonado ◽  
Agustin Gonzalez-Fontes
Keyword(s):  
Enzyme Activities ◽  
Nitrogen Sources ◽  
Carbohydrate Content ◽  
Anabaena Variabilis
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