Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

After irradiation of chick embryos and chicks (1,000 rad), the activity of some erythrocyte enzymes undergoes significant changes. During the 1st day after irradiation of chick embryos, the activity of lactate dehydrogenase leucine aminopeptidase and glutamate pyruvate transaminase decreases. At the 3rd day, the decrease in the activity of glucose-6-phosphate dehydrogenase and acid phosphatase is also observed. In irradiated chicks, the activity of lactate dehydrogenase, leucine aminopeptidase and aldolase decreases within the 1st and the 3rd days, the decrease being most significant for the former two enzymes. At later period (10 and 15 days after irradiation), most significant decrease was found in the activity of glucose-6-phosphate dehydrogenase. The activity of the same enzymes in the blood plasma of irradiated embryos and chicks increases, the increase being most evident for glucose-6-phosphate dehydrogenase.
 ...
PMID:[Activity of several erythrocyte enzymes in chick embryos and chicks after gamma-irradiation]. 65 15

Experimental head injuries, which are easily reproducible in animal studies with guinea pigs, result in a significant increase of secondary serum enzymes. Malate dehydrogenase (MDH), fructose 1,6-diphosphate-aldolase and lactate dehydrogenase (LDH), together with the isoenzymes 1 and 2, are found especially in brain in large amounts. These enzymes act as 'tracer substances' of cerebral tissue and show significantly increased serum activities in cases where acute substantial damage to the brain associated with severe alterations of the blood-brain barrier is found. In the absence of shock, hypoxia and additional bodily injuries the loss of brain tissue has to be considered the only source of enzyme outflow. The early treatment of injured animals with high doses of dexamethasone results in a protective and stabilizing effect, preventing the extrusion of enzymes from the traumatically involved brain cells. Thus by observing the characteristic serum enzyme activities of treated and untreated injured animals a therapeutic effect of dexamethasone can be demonstrated within a relatively short time.
 ...
PMID:Therapeutic effect of dexamethasone in experimental head injuries. 67 78

Hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase activities were determined in the kidney of the aging cat. Kidneys from 24 domestic cats 2 months to 7.5 years old in 6 age groups were examined by light microscopic and histochemical methods. Enzyme activities in anatomic components of the kidney were assessed on a quantitative basis for evaluation of mean activity between the age groups. In the cats with advancing age, renal components generally had stable activity. A significant (P less than 0.05) increase in hexokinase activity occurred with advancing age in the ascending part of the renal loop (Henle's loop) and in the distal convoluted tubule. Significant (P less than 0.05) increases in aldolase activity with aging were in cortical connective tissue, internal part of the glomerular capsule (podocytes), distal convoluted tubule, and convoluted segment (Pi) of the proximal portion of the nephron tubule. L-alpha-glycerophosphate dehydrogenase and lactate dehydrogenase activity increased significantly with aging in the convoluted (Pi) segment of the proximal portion of the nephron tubule.
 ...
PMID:Kidney in the aging cat: hexokinase, aldolase, L-alpha-glycerophosphate dehydrogenase, and lactate dehydrogenase histochemistry. 69 42

It is shown that on the 27-30th day of pregnancy in the myometrium cytoplasm of female rabbits the content of proteins, the aldolase (EC 4.1.2.7) and lactate dehydrogenase (EC 1.1.1.27) activities are increased. Redistribution between fractions of certain lactate dehydrogenase (LDH) isoenzymes is observed: the fraction of LDH4--5 increases and that of LDH1--2 decreases, and the ATPase (EC 3.6.1.3) activity lowers as well. A rise in the amount of proteins in the female rabbits myometrium cytoplasm in the last days of pregnancy and the growing fraction of LDH4--5 testify to the myometrium enchanced contractility during the labour.
 ...
PMID:[Composition and enzymic activity of cytoplasmic proteins in myometrium of female rabbits during pregnancy]. 72 91

The activities of lactate dehydrogenase (LDH), fructose-1.6-diphosphate aldolase (ALD), aspartate aminotransferase (AspAT), alkaline phosphatase (AP), and N-acetyl-beta-glucosaminidase (NAG) were determined on the basis of 75 synovia samples taken from the tarsal joints (Art. talocruralis) of 41 cattle for slaughter of different sexes and aged between one and 13 years as well as on the basis of 56 synovia samples taken from the knee joints (Art. femoropatellaris), tarsal joints (Art. talocruralis), and carpal joints (Art. intercarpicus) of 20 fattening pigs. Both the general condition and cell content of synovial fluid in clinically intact joints are described. The activities of ALD and AspAT (less than 15 IU/l), LDH (less than 200 IU/l), and NAG (less than 6,000 IU/l) in synovial fluid of cattle were much lower than those in blood serum of the same species. They were normally distributed. AP activity (less than 150 IU/l) in synovial fluid, however, was higher by several factors as compared to activity in blblished. In swine synovial AspAT and AP activities were just as high as in blood serum, while LDH activities were higher by 1.5 times. Major NAG activity was observed, as well. All enzyme activities were characterised by normal distribution. All five LDH isoenzymes but only one AP isoenzyme were established. The above data were compared with findings reported by other authors, and the comparison showed these results as being characteristic of synovial enzyme activities in clinically intact joints of the two species under review.
 ...
PMID:[Occurrence of various enzymes in synovial fluid of cattle and swine]. 74 40

Seven enzymes of the Embden-Myerhof pathway of glycolysis were assayed in hypotonically treated epididymal sperm from mature rabbits. These were: fructose-biphosphate aldolase, triosephosphate isomerase, glyceraldehydephosphate dehydrogenase, 3-phosphoglyceromutase, enolase, pyruvate kinase, and lactate dehydrogenase. These enzymes were firmly enough bound to the cell structure to resist removal by washing after hypotonic treatment and had maximal activities comparable to, or greater than, the rate of mitochondrial pyruvate oxidation, so that rapid oxygen uptake was observed with intermediates of the glycolytic pathway. The activity of lactate dehydrogenase in a typical preparation of hypotonically treated cells was 5.3 mumoles/minute x 10(9) cells at 25 degrees C for pyruvate reduction in the hypotonically treated cells and 4.8 mumoles/minute x 10(9) cells in the thrice-washed hypotonically treated cells. The Km for pyruvate was 1.4 mM while that for lactate was 4.4 mM. By contrast, the maximal activity of pyruvate oxidation by mitochondria was 0.10 microgram atom of oxygen/minute x 10(9) cells, corresponding to 0.020 mumole of pyruvate/minute x 10(9) cells, and the Km for pyruvate was 5 microM. These enzyme parameters favor high lactate production from glucose in aerobic glycolysis.
 ...
PMID:Energy metabolism of spermatozoa. V. The Embden-Myerhof pathway of glycolysis: activities of pathway enzymes in hypotonically treated rabbit epididymal spermatozoa. 80 42

The intraccellular proteins of animal cells are continuously turning over; therefore, the concentration of a given protein is regulated both at the level of protein synthesis and at the level of protein degradation. Studies on the relative rates of turnover of isoenzymes, such as those of aldolase and lactate dehydrogenase, may help to clarify the mechanisms involved in protein turnover. The isoenzymes and subunit types are very similar proteins, and are located within the same intracellular compartments; yet, the concentrations of these proteins are independently regulated. The present paper describes the roles of synthesis and degradation in regulating aldolase isoenzyme concentrations in avian brain...
 ...
PMID:Synthesis and degradation of fructose diphosphate aldolase isoenzymes in avian brain. 80 77

The paper described the findings of the activity of aspartate amino transferase (GOT) and alanine amino transferase (GPT), lactate dehydrogenase (LDH), alkaline phosphatase (AP), and aldolase in the blood serum of calves examined for white-muscle disease (WMD). Relapsing mass accurrence of the disease was reported from various agricultural enterprises where calves were fed a milk replacer without vitamin E. In comparison with clinically healthy calves fed a feed mixture with vitamin E, calves suffering from the clinical form of WMD showed an alkaline phosphatase level decrease from 32.3 +/- 7.6 u. K. A. to 15.1 +/- 8.2 u. K. A. On the other hand, the activites of ALD, GOT, GPT, and LDH showed a statistically significant increase. The acute and sub-acute course of the disease increased enzyme activities as follows: ALD from 4.2 +/- 1.1 mumol (= 70.0 +/- 17.0 i.u.) to 9.7 +/- 2.1 mumol (= 163.0 +/- 33.2 i. u.), GOT from 0.9 +/-0.5 mumol (= 68.0 +/- 5.8 i.u.) to 16.7 +/- 11.7 mumol (= 567.0 +/-40.0 i. u.) GPT from 0.2 +/- 0.8 mumol (= 5.0 +/- 12.4 i. u.) to 9.8 +/- 2.8 mumol (= 330.0 +/- 40.4 i.u.), LDH from 46.1 +/- 5.4 mumol (= 765.0 +/- 40.0 i.u.) to 72.7 +/- 24.3 mumol (= 1,207.0 +/- 403.0 i.u.). In WMD-affected herds, similar enzyme activity fluctuations were observed even in calves showing no clinical signs of the disease. It follows from the study that the examination of serum enzymes provides a method to demonstrate the clinical and pre-clinical forms of white-muscle disease and that it can be included in the set of tests for the diagnosis of diseases in calves. The significant differences in all calves in the affected herds show that the disease is a danger to all animals in the herd fed a deficient mixture.
 ...
PMID:[Activity of some serum enzymes in calves suffering from white muscle disease]. 81 57

The paper described the findings of the activity of aspartate amino transferase (GOT) and alanine amino transferase (GPT), lactate dehydrogenase (LDH), alkaline phosphatase (AP), and aldolase in the blood serum of calves examined for white-muscle disease (WMD). Relapsing mass accurrence of the disease was reported from various agricultural enterprises where calves were fed a milk replacer without vitamin E. In comparison with clinically healthy calves fed a feed mixture with vitamin E, calves suffering from the clinical form of WMD showed an alkaline phosphatase level decrease from 32.3 +/- 7.6 u. K. A. to 15.1 +/- 8.2 U. K. A. On the other hand, the activities of ALD, GOT, GPT, and LDH showed a statistically significant increase. The acute and subacute course of the disease increased enzyme activities as follows: ALD from 4.2 +/- 1.1 mumol (= 70.0 +/- 17.0 i. u.) to 9.7 +/- 2.1 mumol (= 163.0 +/- 33.2 i. u.), GOT from 0.9 +/- 0.5 mumol (= 68.0 +/- 5.8 i. u.) to 16.7 +/- 11.7 mumol (= 567.0 +/- 40.0 i. u.), GPT from 0.2 +/- 0.8 mumol (= 5.0 +/- 12.4 i. u.) to 9.8 +/- 2.8 mumol (= 330.0 +/- 40.4 i. u.), LDH from 46.1 +/- 5.4 mumol (= 765.0 +/- 40.0 i. u.) to 72.7 +/- 24.3 mumol (= 1,207.0 +/- 403.0 i. u.). In WMD-affected herds, similar enzyme activity fluctuations were observed even in calves showing no clinical signs of the disease. It follows from the study that the examination of serum enzymes provides a method to demonstrate the clinical and pre-clinical forms of white-muscle disease and that it can be included in the set of tests for the diagnosis of diseases in calves. The significant differences in all calves in the affected herds show that the disease is a danger to all animals in the herd fed a deficient mixture.
 ...
PMID:[Activity of various serum enzymes in calves suffering from nutritionally-induced muscular dystrophy]. 81 73

Treatment with the polyene antibiotic, filipin, renders the spermatozoan cell membrane permeable to small molecules, but not to the intracellular enzymes aldolase and lactate dehydrogenase. Pyruvate (10 mM) as the sole substrate was metabolized very slowly. L-Carnitine increased pyruvate metabolism 3- to 4-fold and allowed limited rates of oxidative phosphorylation. When spermatozoa treated with filipin were supplemented with malate, there was a rapid, almost linear rate of pyruvate metabolism which was slightly increased by L-carnitine. In the absence of malate, 20 to 30% of the pyruvate used was reduced to lactate; this increased to 57% in the presence of malate. Without malate, about 90% of the pyruvate metabolized was converted to lactate and acetate or L-acetylcarnitine. Rutamycin or rotenone increased both the rate of pyruvate use and the delta lactate/deltapyruvate ratio. Under all treatments, L-carnitine consistently reduced the percentage of pyruvate converted to lactate by about 10%; part of the pyruvate was preferentially shunted into L-acetylcarnitine rather than lactate. The mitochondrial inhibitors, rotenone or rutamycin, did not change the amount of pyruvate that was converted to metabolites other than lactate, or L-acetylcarnitine, or both. Pyruvate-supported State 3 respiration was linear only if L-carnitine, or malate, or both, were added to the incubation medium. Added malate was necessary to produce a rapid State 3 respiratory rate and was also required for significant respiratory activity in the presence of rotenone or rutamycin. From cells metabolizing [2-14C]pyruvate (1.4 mM), 14C-labeled acid-extractable metabolites were separated by ion exchange column chromatography. All of the [2-14C]pyruvate (+/-5%) used was recovered in 14C-labeled metabolites and 14CO2. In the presence of malate, citrate accumulation was significant, and was always large in comparison to flux through the citric acid cycle. Glutamate, beta-hydroxybutyrate, acetoacetate, fumarate, aspartate, and alpha-ketoglutarate did not accumulate in significant amounts. Some 14C-labeled succinate was produced but only in the presence of malate. Alkaline hydrolysis of a fraction containing carnitine esters yielded acetate and a compound tentatively identified as beta-hydroxybutyrate or lactate. As in intact cells, intramitochondrial lactate dehydrogenase competes successfully with the electron transport system for the NADH generated by pyruvate metabolism. The role of lactate and L-carnitine, and conclusions suggested by the accumulation of certain metabolites are discussed in relation to control of citric acid cycle activity.
 ...
PMID:Mitochondrial metabolism of pyruvate in bovine spermatozoa. 83 19


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>