Time course of ammonia release and binding and of acid proteinase and glycolytic enzyme activity during experimental toxico-adrenal encephalopathy

1988 ◽  
Vol 105 (1) ◽  
pp. 33-35
Author(s):  
V. M. Kovalenko ◽  
R. A. Trapezontseva ◽  
G. A. Vilkov
Keyword(s):  
Enzyme Activity ◽  
Time Course ◽  
Glycolytic Enzyme ◽  
Acid Proteinase ◽  
Ammonia Release

scholarly journals Rat uterine microbiochemistry: metabolic enzyme activities stimulated by 17-beta-estradiol are localized in epithelial cells.

1987 ◽  
Vol 35 (6) ◽  
pp. 657-662 ◽  
Author(s):  
J P Holt ◽  
E Rhe
Keyword(s):  
Enzyme Activity ◽  
Smooth Muscle ◽  
Epithelial Cells ◽  
Dose Response ◽  
Enzyme Activities ◽  
Time Course ◽  
Citrate Synthase ◽  
Ovariectomized Rats ◽  
Similar Response ◽  
Estradiol Treatment

Lactate dehydrogenase (LDH; EC 1.1.1.27), citrate synthase (CS; EC 4.1.3.7), and beta-hydroxyacyl-CoA-dehydrogenase (beta-OH-acyl-CoA-DH; EC 1.1.1.35) activities were determined in each of the three major cell types of rat uterus, i.e., epithelial, stromal, and smooth muscle, using quantitative microanalytical techniques. Adult ovariectomized rats were treated with 17-beta-estradiol to determine the time course and dose response (0.025-50 micrograms/300-g rat) effect of estrogen on enzyme activity of each type of uterine cell. The use of "oil well" and enzyme-cycling microtechniques to determine the time course and the dose responses of enzyme activity changes required microassays involving 1595 microdissected single cell specimens. Estradiol treatment increased epithelial LDH, CS and beta-OH-acyl-CoA-DH activity but had no effect on these enzymes in the stroma or in smooth muscle cells. The estradiol-stimulated peak enzyme activities on Day 4 in the intervention group are compared with those in the ovariectomized rat controls as follows: LDH, 44.5 +/- 3.5 vs 22.3 +/- 3.9; CS, 3.5 +/- 0.2 vs 1.5 +/- 0.6; beta-OH-acyl-CoA-H, 3.5 +/- 0.32 vs 2.2 +/- 0.2 (mean +/- standard deviation; mol/kg/hr). Stromal cell activities (LDH, 7.4 +/- 1.0; CS, 1.2 +/- 0.2; beta-OH-acyl-CoA-DH, 0.9 +/- 0.1) were significantly lower than epithelial cell levels and were similar to smooth muscle levels. Therefore, even in the ovariectomized animal epithelial cells have markedly higher metabolic activity compared with adjacent cells. The enzyme activities are expressed as moles of substrate reacting per kilogram of dry weight per hour. All three enzymes exhibited a 17-beta-estradiol-induced dose response between 0.025-0.15 micrograms/300-g rat. The three enzymes studied all had similar response patterns to estrogen. The effect of estradiol was restricted to epithelial cells, with enzyme activities increasing to maximal levels after approximately 96 hr of hormone treatment. This study therefore not only confirms the specific and differential metabolic responses of uterine cells to estradiol treatment, but clearly demonstrates that marked metabolic differences exist between epithelial cells and stromal or smooth muscle uterine cells.

Differential recovery of acetylcholinesterase in guinea pig muscle and brain regions after soman treatment

1998 ◽  
Vol 17 (3) ◽  
pp. 157-162 ◽  
Author(s):  
Maxine C Lintern ◽  
Janet R Wetherell ◽  
Margaret E Smith
Keyword(s):  
Enzyme Activity ◽  
Time Course ◽  
Brain Regions ◽  
Similar Rate ◽  
Molecular Forms ◽  
Similar Degree ◽  
Brain Areas ◽  
Pig Muscle ◽  
Rate Of Recovery ◽  
The Brain

1 In brain areas of untreated guinea-pigs the highest activity of acetylcholinesterase was seen in the striatum and cerebellum, followed by the midbrain, medulla-pons and cortex, and the lowest in the hippocampus. The activity in diaphragm was sevenfold lower than in the hippocampus. 2 At 1 h after soman (27 mg/kg) administration the activity of the enzyme was dramatically reduced in all tissues studied. In muscle the three major molecular forms (A12, G4 and G1) showed a similar degree of inhibition and a similar rate of recovery and the activity had returned to normal by 7 days. 3 In the brain soman inhibited the G4 form more than the G1 form. The hippocampus, cortex and midbrain showed the greatest reductions in enzyme activity. At 7 days the activity in the cortex, medulla pons and striatum had recovered but in the hippocampus, midbrain and cerebellum it was still inhibited. 4 Thus the effects of soman administration varied in severity and time course in the different tissues studied. However the enzyme activity was still reduced in all tissues at 24 h when the overt signs of poisoning had disappeared.

Relation Between Acid Proteinase Activity and Redistribution of Nitrogen During Grain Development in Wheat

1976 ◽  
Vol 3 (6) ◽  
pp. 721 ◽  
Author(s):  
MJ Dalling ◽  
G Boland ◽  
JH Wilson
Keyword(s):  
Enzyme Activity ◽  
Nitrogen Removal ◽  
Nitrogen Loss ◽  
Proteinase Activity ◽  
Acid Proteinase ◽  
Wheat Cultivars ◽  
Grain Development ◽  
Significant Relation ◽  
Activity Measurements ◽  
Grain Nitrogen

Accumulation of grain nitrogen was studied in the wheat cultivars Argentine IX and Insignia. The pattern of nitrogen removal from several tissues of each cultivar was compared with the pattern of acid proteinase activity. There was a highly significant relation between the rate of nitrogen loss from the tissues and the rate estimated from the enzyme activity measurements. This suggests an important role for acid proteinase enzymes in leaf senescence. Redistribution of nitrogen present in the plant at anthesis accounted for 78.5 and 80.6 % of the final grain nitrogen yield of Argentine IX and Insignia respectively.

scholarly journals Glycolytic Enzyme Activity Is Essential for Domestic Cat (Felis catus) and Cheetah (Acinonyx jubatus) Sperm Motility and Viability in a Sugar-Free Medium1

2011 ◽  
Vol 84 (6) ◽  
pp. 1198-1206 ◽  
Author(s):  
Kimberly A. Terrell ◽  
David E. Wildt ◽  
Nicola M. Anthony ◽  
Barry D. Bavister ◽  
S.P. Leibo ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Sperm Motility ◽  
Glycolytic Enzyme ◽  
Felis Catus ◽  
Domestic Cat ◽  
Acinonyx Jubatus

4-26-05 Muscle mitochondrial and glycolytic enzyme activity in critically ill patients

1997 ◽  
Vol 150 ◽  
pp. S243
Author(s):  
A. Papadimitriou ◽  
R. Divari ◽  
E. Kouremenos ◽  
M. Tsamouri ◽  
P. Stefanidis ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Critically Ill ◽  
Critically Ill Patients ◽  
Glycolytic Enzyme

scholarly journals The androgenic regulation of superhelical-DNA nicking-closing enzyme in rat ventral prostate

1981 ◽  
Vol 196 (1) ◽  
pp. 195-202 ◽  
Author(s):  
J D Filipenko ◽  
P S Rennie ◽  
N Bruchovsky
Keyword(s):  
Enzyme Activity ◽  
Dna Synthesis ◽  
Chromatin Structure ◽  
Structural Organization ◽  
Time Course ◽  
Ventral Prostate ◽  
Rat Ventral Prostate ◽  
Dna Nicking ◽  
Androgenic Regulation

The activity of superhelical-DNA nicking-closing enzyme (NC enzyme) was measured in nuclei from rat ventral prostate by a fluorimetric assay based on the binding of ethidium bromide to supercoiled phage-PM2 DNA. The nuclear concentration of NC-enzyme activity declined rapidly after castration, although this response could be prevented by daily administration of dihydrotestosterone. The low NC-enzyme activity in involuted prostates (10% of normal) was restored to normal after 8-10 days of treatment with androgen. In the regenerating prostate the time course of restoration of NC-enzyme activity was not in phase with that of DNA synthesis. Examination of nucleosome repeat lengths and the arrangement of nucleosomes along the chromatin fibre revealed no differences in the structural organization of chromatin in prostates with high or low NC-enzyme activity. Together, these results suggest that the major role of NC enzyme is related to the onset and maintenance of differentiation in the prostate and that the activity of this enzyme is not expressed through gross alterations in chromatin structure.

scholarly journals Regional enzyme development in rat brain. Enzymes associated with glucose utilization

1984 ◽  
Vol 218 (1) ◽  
pp. 131-138 ◽  
Author(s):  
S F Leong ◽  
J B Clark
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Rat Brain ◽  
Brain Regions ◽  
Glycolytic Enzyme ◽  
Glycolytic Potential ◽  
Key Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Potential Enzyme Activity ◽  
The Brain

The development of key enzyme activities concerned with glucose metabolism was studied in six regions of the rat brain in animals from just before birth (-2 days) through the neonatal and suckling period until adulthood (60 days old). The brain regions studied were the cerebellum, medulla oblongata and pons, hypothalamus, striatum, mid-brain and cortex. The enzymes whose developmental patterns were investigated were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49). Hexokinase, aldolase and lactate dehydrogenase activities develop as a single cluster in all the regions studied, although the timing of this development varies from region to region. Glucose-6-phosphate dehydrogenase activity, however, declines relative to glycolytic enzyme activity as the brain matures. When the different brain regions are compared, it is clear that the medulla develops its glycolytic potential, as indicated by its potential enzyme activity, considerably earlier than the other regions (hypothalamus, striatum and mid-brain), with the cortex and cerebellar activities developing even later. This enzyme developmental sequence correlates well with the neurophylogenetic development of the brain and adds support to the hypothesis that the development of the potential for glycolysis in the brain is a necessary prerequisite for the development of neurological competence.

scholarly journals Molecular cloning and regulatory analysis of the arylsulfatase structural gene of Neurospora crassa.

1989 ◽  
Vol 9 (9) ◽  
pp. 3630-3637 ◽  
Author(s):  
J V Paietta
Keyword(s):  
Enzyme Activity ◽  
Neurospora Crassa ◽  
Time Course ◽  
Constitutive Expression ◽  
Temperature Sensitive ◽  
Polymorphism Analysis ◽  
Regulatory Mutant ◽  
Coordinate Control ◽  
Arylsulfatase Activity ◽  
Regulatory Analysis

The ars-1+ gene of Neurospora crassa encodes the enzyme arylsulfatase. ars-1+ is in a group of highly regulated sulfur-related structural genes that are expressed under conditions of sulfur limitation and are under coordinate control of the cys-3+ and scon+ regulatory genes. The ars-1+ gene was cloned by chromosome walking from the qa gene cluster, using a lambda library. Cotransformation of an N. crassa ars-1 mutant with the isolated lambda clones and the benomyl resistance gene, followed by assay for arylsulfatase activity, was used to screen for the ars-1+ gene. Further confirmation that the cloned segment mapped to the ars-1+ locus was obtained by restriction-fragment-length polymorphism analysis. Northern (RNA) blot analysis showed that the ars-1+ gene was transcribed to give an mRNA of 2.3 kilobases. In wild-type cells, the ars-1+ transcript was abundant under sulfur-derepressing conditions but absent under repressing conditions. Time course analysis showed that the appearance of ars-1+ message in sulfur-derepressed cultures paralleled the appearance of arylsulfatase enzyme activity. In addition, transcription of ars-1+ was detected only under derepressing conditions in a nuclear transcription assay. In a cys-3 regulatory mutant that was unable to synthesize arylsulfatase (or other sulfur-controlled enzymes), there was no ars-1+ transcript under repressing or derepressing conditions. In a temperature-sensitive cys-3 mutant, the ars-1+ transcript was present only at the permissive growth temperature and under sulfur derepression. A negative regulatory mutant, sconc, displayed both constitutive expression of arylsulfatase enzyme activity and content of ars-1+ message.

Sign in / Sign up

Export Citation Format

Share Document