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

An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze-dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI), malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose-6-phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), alpha-glycerophosphate dehydrogenase (alpha-GOPDH), hexokinase (HK), and phosphofructokinase (PRK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of relication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.
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PMID:Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors. 20 41

Extracts of the horse and sheep strains of Echinococcus granulosus and E. multilocularis were compared on the basis of their isoenzyme patterns for 10 enzymes by means of isoelectric focusing in polyacrylamide gels. The enzymes examined were: acid phosphatase, lactate dehydrogenase, malate dehydrogenase, malic enzyme, phosphoglucoseisomerase, isocitrate dehydrogenase, adenylate kinase, aldolase and alpha-glycerophosphate dehydrogenase. Interspecific and intraspecific differences are apparent in the isoenzyme profiles of all the enzymes except adenylate kinase; the pattern and activity of adenylate kinase are identical for both strains of E. granulosus but this enzyme clearly distinguishes these forms from E. multilocularis. The absence of electromorphic variation in any of the enzymes from either form of E. granulosus may be a result of the self-fertilizing hermaphraditism of these organisms.
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PMID:Isoelectric focusing of some enzymes from Echinococcus granulosus (horse and sheep strains) and E. multilocularis. 47 21

1. Enzyme activities were studied in blood plasma from Rhenish, Italian, Landes and Masseubian geese. 2. Strains used for liver production (Landes, Masseubian) showed higher activities of aspartate transaminase (AST) [EC 2.6.1.1], alanine transaminase (ALT) [EC 2.6.1.2] and fructose aldolase (FRA) [EC 4.1.2.13] while breeds with high egg production (Rhenish, Italian) had higher activities of both alkaline phosphatase (ALP) [EC 3.1.3.1] and acid phosphatase (ACP) [EC 3.1.3.2]
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PMID:Blood enzyme activities in different breeds of geese. 49 70

Studies on organ homogenates of 22 one-year-old healthy geese indicated ubiquiternal distribution of GOT and GPT transaminases, lactate dehydrogenase, alkaline and acid phosphatase, aldolase and kreatine phosphokinase, without the presence of any pronounced organ specificity of some of the named enzymes. It is presumed that the investigation on these enzymes in goose blood serum can be of use only for determining the degree and the course of a given disease, but not for organ-localization of the disease's process.
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PMID:[Enzymatic activity study of the organs and blood serum of geese]. 53 93

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.
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PMID:[Activity of several erythrocyte enzymes in chick embryos and chicks after gamma-irradiation]. 65 15

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

The activities of aspartate transminase (EC 2.6.1.1), alanine transminase (EC 2.6.1.2), alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2) leucine arylamidase (EC 3.4.1.1), aldolase (EC 4.1.2), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.38) and cholinesterase (EC 3.1.1.7) were measured in serum of male rabbits and albino Wistar rats in dlplicate by means of microliter techniques. Furthermore, the diurnal alterations of enzyme activity were established in 8--10 animals of both species. Aspartate transaminase activity in the serum of rats was found to be significantly higher than in the serum of humans and rabbits, and essentially lower alkaline phosphatase values were obtained from the serum of rabbits in comparison with those found for the serum of humans and rats. Relatively high acid phosphatase and aldolase values as well as a very low cholinesterase activity were found in the serum of rabbits and rats. The mean malate dehydrogenase-activity was found to be twice as high as the mean lactate dehydrogenase, which is the contrary of the situation found in human serum. No significant diural alterations of the examined enzyme activities were established. The differences found between the animal and the human enzyme activities in serum are explained by species-determined peculiarities of metabolism or specific enzyme configuration.
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PMID:[Enzyme activities in serum of rabbits and rats-reference values and circadian alterations. Serum enzymes and factors that influence their activity,I (AUTHOR'S TRANSL)]. 103 68

Streptolysin O was measured in subcellular fractions of group A streptococci obtained after preparation of protoplasts in a hypertonic buffer containing raffinose. Most of the activity was located in the periplasm (the region between cell wall and membrane) and did not differ in several characteristics from that of extracellular streptolysin O. Of the enzymes used as subcellular markers, aldolase and maltase (cytoplasmic) and acid phosphatase (membrane associated) were in the same fractions as found in other bacteria. However, the location of alkaline phosphatase differed from that of other bacteria in the most of the activity was in cytoplasm rather than in the periplasm.
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PMID:Cellular location of streptolysin O. 110 77

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

Studied were the changes in the values of some hematologic indices (hemoglobin, erythrocytes, leukocites) as well as the values of some biochemical (total protein and protein fractions, urea, total lipids, bilirubin, inorganic, phosphorus calcium) and enzyme factors (lactatedehydrogenase, alkaline and acid phosphatase, aldolase, amino transferrases, creatinephosphokinase) in geese prior to and after experimental infection of Borrelia anserina. It was found that in the peak stage of spirochetemia the content of hemoglobin, total lipids, and calcium, the percent of albumins and alfa-globulins, and the activity of the alkaline phosphatase in the blood decreased. The prealbumin fraction of the serum protein was completely reduced. The activity of the lactatedehydrogenase, acid phosphatase, amino transferrases, and aldolase showed higher values that were statistically significant, while the activity of the creatinephosphokinase rose to a slighter extent. The urea, bilirubin, inorganic phosphorus, and the alfa-, beta-, and gamma-globulins correlated positively with the course of the infection.
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PMID:[Biochemical changes in the blood of geese infected with Borrelia anserina]. 117 37


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