Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The isozyme patterns and activities of six enzymes were determined in surgical biopsy samples of lung tumors and non-neoplastic pulmonary areas. Fetal lungs were also examined. No tissue differences were found in the isozyme pattern of hexokinase or alkaline phosphatase; small differences in pyruvate kinase isozyme proportions were observed. The tumors exhibited significant deviations with respect to the lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) isozyme patterns. Despite the diversity of cell types, the proportions of the M-subunit of LDH in each tumor and that of the mitochondrial isozyme of MDH in all but one tumor were higher than in control samples from the same lung. In contrast, the normal fetal lung showed a higher LDH-H proportion than did adult lung and a mature MDH isozyme pattern. The alpha-glycerophosphate dehydrogenase and adenylate kinase activities of the tumors were about one-tenth and one-fourth, respectively, of those of nonneoplastic adult lung. These lower activities (evident also in normal fetal lung) were accompanied by 3- to 5-fold increases in the LDH, MDH, pyruvate kinase, and hexokinase activities of the tumors; fetal lungs had lesser increases (2- to 3-fold) for the first 3 enzymes. The common features of tumors with different cell types and histological grade identified here point to several enzymes the quantitation or isozyme analysis of which may be of practical use in distinguishing cancerous from nonneoplastic human lung samples. A combination of different indicators, such as opposite changes in LDH and alpha-glycerophosphate dehydrogenase activity, coupled with elevated proportions of LDH-M, may be used to diagnose neoplasia most reliably.
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PMID:Enzyme activities and isozyme patterns in human lung tumors. 669 92

Rectal biopsy specimens from control subjects, patients with either active or quiescent ulcerative colitis, and patients with Crohn's colitis were examined histologically and assayed for marker enzymes associated with tissue organelles. They were catalase (peroxisome); neutral alpha-glucosidase (endoplasmic reticulum); alkaline phosphatase (plasma membrane); malate dehydrogenase (mitochondria); lactate dehydrogenase (cytosol). There was no significant change in these enzyme activities in patient samples compared with controls. Activities of three acid hydrolases (lysosomal enzymes), beta-glucuronidase, acid phosphatase, and N-acetyl-beta-glucosaminidase, were also assayed in the biopsy samples. Decreased activities of all three enzymes were noted in ulcerative colitis, particularly in active disease. Normal values were obtained in Crohn's colitis. Measurement of lysosomal integrity by assays of latent N-acetyl-beta-glucosaminidase activity revealed similar results in control and colitic subjects. It is suggested that the lysosomal changes reflect a specific tissue release of enzyme and may be implicated in the pathogenesis of the tissue damage.
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PMID:Organelle pathology in ulcerative and Crohn's colitis with special reference to the lysosomal alterations. 671 88

The circular dichroism bands of (+) gossypol in the spectral region 300-400 nm have been shown to be sensitive to interactions with proteins. Using CD spectroscopy, gossypol has been shown to interact with lactate dehydrogenase, malate dehydrogenase, alkaline phosphatase, lysozyme, protamine and poly-L-lysine. Binding to proteins generally results in a pronounced red shift of the long wavelength CD band (approximately 380-430 nm) accompanied by a reduction in ellipticity. The changes in spectral parameters of the 1Lb binaphthyl transition may reflect a distortion from a nearly perpendicular gossypol conformation, on binding to proteins.
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PMID:A circular dichroism study of (+) gossypol binding to proteins. 674 22

For the purpose of describing early chondrogenic metabolic and structural events, measurements were made of oxidative and other enzymatic activities at various stages in the morphologic development of chondrocytes over a period of 18 to 20 days in continuous cell culture. Comparisons were also made between cells grown in 20% O2 and in 35% O2. These cultures exhibited rapid confluence (within 24 hours), early development of cartilaginous nodules by Day 2 to 3 and metachromatic staining of the chondrocyte matrix by Day 3 to 4. Under 35% O2, cell sheets were thicker and there was increased pleomorphism of chondrocyte and fibroblast cell types, with a relative increase of fibroblast components and reduction in chondroblasts and chondrocyte aggregates. Using the von Kossa staining procedure, calcium salt deposition was observed by Day 9. There was no apparent difference in mineralization of cultures grown under the low and high O2 tensions. Under normoxic conditions cytochrome oxidase and malate dehydrogenase (MDH) activities increased rapidly for the first three to four days and then remained essentially constant. Lactate dehydrogenase (LDH) activity increased continuously over the life of the culture. Acid phosphatase increased rapidly until about Day 13 after which it remained constant, whereas alkaline phosphatase showed a bimodal activity profile. Under hyperoxic conditions, cytochrome oxidase, MDH and alkaline phosphatase activity were significantly inhibited. LDH and acid phosphatase activities were markedly inhibited initially but with time showed a degree of recovery.
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PMID:Development of chick limb bud chondrocytes in cell culture: morphologic and oxidative metabolic observations. 701 57

The activity of serum enzymes, such as, creatine kinase (CK), pyruvate kinase (PK), aldolase (ALD), lactate dehydrogenase (LDH), sorbitol dehydrogenase (SbDH), malate dehydrogenase (MDH), glutamate-aspartate aminotransferase (AST), glutamate-alanine aminotransferase (ALT), myokinase (MK), glucosephosphate isomerase (GPI), alkaline phosphatase (AlkP), pseudocholinesterase (PsCHE) isocitrate dehydrogenase and gamma-glutamyltranspeptidase (gamma-GTP), was determined in 256 patients with progressing myodystrophy (PMD) (Duchenne's form in 125, Becker's form in 14, pelvicohumeral form in 36, humeroscapulofacial form in 19, ocular form in 10, other rare forms in 34, and nonidentified forms in 13 patients). In the control group (64 men, 56 women and 50 children), the activity of the enzymes was found to depend on the patients' sex and age. With regard to both parameters, i. e. the degree of the enzyme activity rise and the frequency of the pathological values the most informative were CK, then PK and ALD, and then all the other enzymes. Of all the PMD forms the enzymatic activity appeared to be the highest in patients with the pseudohypertrophic malignant form. By determining the activity of five enzymes (CK, ALD, LDH, AST and ALT) and taking into consideration the patient's age, the onset and the duration of the disease one can distinguish between sick and healthy subjects, as well as between various forms of PMD.
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PMID:[Serum enzyme dynamics in progressive muscular dystrophies]. 703 17

Portions of jejunal biopsies from control subjects and from patients with coeliac disease were cultured for 24 hours using an in vitro organ culture technique. Alkaline phosphatase activity was measured in the tissue and medium before and after culture; enzyme activities were expressed per microgram tissue DNA. The increase in enzyme activity during the culture period was taken to represent net enzyme synthesis. Alkaline phosphatase synthesis by mucosa from patients with untreated gluten-sensitive coeliac disease and by mucosa from patients with non-responsive coeliac disease was significantly less than that by normal mucosa. Alkaline phosphatase synthesis by mucosa from patients with treated gluten-sensitive coeliac disease was greater than that by untreated coeliac mucosa but was less than normal mucosa. Sequential studies of alkaline phosphatase synthesis by jejunal mucosa from seven patients with coeliac disease, before and after successful treatment by gluten withdrawal, showed an increase in synthesis in all patients. Study, by analytical subcellular fractionation with sucrose density gradient centrifugation, of the properties of the organelles of cultured control tissue showed good preservation of their integrity. A striking finding, however, was the decrease in malate dehydrogenase with a corresponding marked increase in lactate dehydrogenase. This would be expected to be followed by a shift from aerobic to anaerobic metabolism. Analytical subcellular fractionation of cultured mucosa from patients with coeliac disease gave similar conclusions. There was, however, a marked improvement of the brush border abnormalities, characteristic of coeliac disease, during culture with increased enzyme activities and membrane equilibrium density in the sucrose gradients.
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PMID:Alkaline phosphatase synthesis and properties of subcellular organelles during in vitro culture of jejunal biopsies from control subjects and patients with coeliac disease. 706 34

A high dose of niridazole administered intraperitoneally (i.p.) to male rats over a period of 9 weeks induced alterations in the concentrations and activities of some important testicular constituents and enzymes, respectively. The concentrations of total and free cholesterol were higher than those of control animals but the concentration of esterified cholesterol was significantly lower than that of the control rats. Zinc concentration in the testis and prostate gland of niridazole-treated animals was significantly lower than in the control animals. Decreases in the activities of the following enzymes occurred in the testes of niridazole-treated rats: lactate and sorbitol dehydrogenases, aspartate and alanine aminotransferases and alkaline phosphatase. By contrast, there were increases in the activities of testicular malate dehydrogenase and prostate acid phosphatase of rats given niridazole.
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PMID:Niridazole-induced biochemical changes in the rat testis. 716 74

The changes were followed up that take place in the activity of the more important serum enzymes, such as glutamate oxalacetate transaminase, glutamate pyruvate transaminase, serum dehydrogenase, malate dehydrogenase, lactate dehydrogenase, creatine phosphokinase, and alkaline phosphatase, as well as aldolase in the development of the experimental infection with various doses of Taenia ovis eggs in lambs. Used were 14 two-month-old lambs divided into test groups of 4 animals each and a control group of two lambs. In the lambs of three of the test groups infected with 4000, 7000, and 30 000 T. ovis eggs, respectively, no signs were observed of enhanced serum enzyme activity up to the 35th day following infection. Later on there was a drop of the activity of these enzymes however, with the exception of alkaline phosphatase the values of all studied serum enzymes remained higher than the normal ones up to the end of the experiment.
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PMID:[Effect of an experimental infestation with Cysticercus ovis on serum enzyme activity in lambs]. 717 Jul 68

The measured (apparent) specific activities of immobilized lactate dehydrogenase, malate dehydrogenase, glucose dehydrogenase, alkaline phosphatase and chymotrypsin decrease with increasing activity loading and increase with decreasing particle diameter and with increasing substrate concentration. The observed inactivation is therefore concluded to be due to diffusional limitation. Real specific activities are not greatly affected by the immobilization, as has been demonstrated after enzymic digestion of the matrix. In the case of lactate dehydrogenase and of malate dehydrogenase real specific activities are not altered by a variation of the number of bonds to the carrier.
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PMID:Factors affecting the activity of immobilized enzymes, I. Diffusional limitation. 742 23

Changes in oxidative metabolism were studied in hepatopancreas, muscle, and hemolymph of the edible crab Scylla serrata, exposed to a sublethal concentration (2.5 ppm) of cadmium chloride. A significant decrease in glycogen, total carbohydrates, and pyruvate and an increase in lactate levels in hepatopancreas and muscle were observed. Hemolymph sugar levels were increased in experimental crabs. An increase in phosphorylase suggested increased glycogenolysis during cadmium toxicity. The decrease in lactate dehydrogenase activity and the increase in lactate content indicated reduced mobilization of pyruvate into the citric acid cycle. Krebs cycle enzymes such as succinate dehydrogenase and malate dehydrogenase were found to be decreased, suggesting impairment of mitochondrial oxidative metabolism as a consequence of cadmium toxicity. Glucose-6-phosphate dehydrogenase activity was increased, suggesting enhanced oxidation of glucose by the HMP pathway. Cytochrome-c oxidase and Mg2+ ATPase activity levels decreased, indicating impaired energy synthesis during cadmium stress. Acid and alkaline phosphatase activities increased, suggesting enhanced breakdown of phosphates to release energy in view of impaired ATPase system during cadmium exposure. A significant decrease in protein and free amino acid and an increase in ammonia, urea, and glutamine levels were observed in the tissues during exposure. An increase in protease, alanine aminotransaminase, and aspartate aminotransaminase suggested increased proteolysis and transamination of amino acids. The increase in glutamate dehydrogenase, AMP deaminase, and adenosine deaminase indicated increased ammonia production. The increased arginase and glutamine synthetase suggested the detoxification or mobilization of ammonia toward the production of urea and glutamine. These results suggest that cadmium affects oxidative metabolism and induces hyperammonemia, and crabs switch over their metabolic profiles toward compensatory mechanisms for the survivability in cadmium-polluted habitats.
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PMID:Changes in oxidative metabolism in selected tissues of the crab (Scylla serrata) in response to cadmium toxicity. 753 86


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