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 genetic structure of three Asiatic eskimos subpopulations (402 individuals), five coast chuckchies subpopulations (1793 individuals) and three reindeer chuckchies subpopulations (559 individuals) have been studied for 26 electrophoretic protein systems (33 loci). These are: adenilate-kinase (AK), diaphorase NAD X H (Dia), glyoxalase-1 (GLO-1), glucose-6-phosphate dehydrogenase (6GPT), glutamatpyruvate transaminase (GPT), glutamicoxalate transaminase (GOT), carbonic anhydrase-1 (Ca-1), catalase (Ct), acid phosphatase (AcP), lactate dehydrogenase (loci LDH-A and LDH-B), leucine aminopeptidase (Lap), malatedehydrogenase (MDH), purine nucleoside phosphorylase (PNP), superoxide dismutase (Sod), 6-phosphogluconate dehydrogenase (PGD), phosphoglucomutase (loci PGM1 and PGM2), cholinesterase (loci c1--c5), alkaline phosphatase (Pp), esterase D (EsD), red cell esterase (Est) - 4 loci, albumin (Alb), haptoglobin (Hp), hemoglobine (Hb A and B), group-specific component (Gc), transferrin (Tf), ceruloplasmin (Cp). In addition, AB0 and Rh system blood groups and phenyl thiocarbamide taste sensitivity (PTC) have been studied. 12 of 36 loci are polymorphic (33.33%), heterozygosity for all loci in eskimos, coastal and reindeer chuckchies being 0.118 +/- 0.005, 0.130 +/- 0.002 and 0.120 +/- 0.004, respectively. These estimates do not differ essentially from heterozygosity at these loci for mongoloid groups living further south. The test for interpopulation heterogeneity has permitted to estimate contribution of the loci to the differentiation of these populations. The least heterogeneity has been found at loci where gene frequency distribution is the most specific for these ethnic groups.
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PMID:[Genetic structure of the populations of native inhabitants in the northeastern USSR. III. Asiatic Eskimos and the coast and reindeer Chukchi]. 643 3

Five min after administration of a single, i.p. dose of ammonium metavanadate (5 mg/kg), in rats, liver enzyme activities were measured. Microsomal mixed-function oxidases (except for aminopyrine N-demethylase), glucose-6-phosphatase and alkaline phosphatase were inhibited but lactate, malate, and glycerophosphate dehydrogenases as well as microsomal NADPH2-dependent cytochrome c reductase were unchanged.
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PMID:Effects of ammonium metavanadate on rat liver enzymes. 660 66

The activities of alkaline phosphatase and reduced nicotinamide adenine dinucleotide (NADH) diaphorase in the principal cells of the guinea pig epididymis were studied histochemically. Alkaline phosphatase activity was absent from the principal cells but was present in the basement membrane of the epididymal epithelium. NADH diaphorase activity was distributed throughout the cytoplasm of the principal cells in each epididymal segment. There was a gradual increase in NADH diaphorase activity from segments 1 through 7. Possible functions of alkaline phosphatase and NADH diaphorase in the epididymis are discussed.
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PMID:Localization of alkaline phosphatase and NADH diaphorase in the principal cells of the guinea pig epididymis. 668 19

Parallel stereo- and cytospectrophotometric examinations of human myocardial capillaries, 20-60 min after biological death were carried out. The activity of alkaline phosphatase, adenosine triphosphatase, lactate dehydrogenase and NAD-diaphorase in the capillary wall in relation to the sex and age in cardiovascular pathology, renal diseases and leukemias were studied. The permeability and level of energy supply of transendothelial transport were found to depend on the kind of the main pathological process and type of death. According to the parameters under study, the functional state of the capillary network of the myocardium in atherosclerosis with or without its combination with hypertension and also in secondary renal hypertension is described.
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PMID:[Stereological characteristics and enzymatic activity of myocardial capillaries in different variants of pathology and death (data from immediate autopsies)]. 686 Jan 68

The article deals with the results of histochemical study of some redox and proteolytic enzymes (SDH, MDH, NAD-diaphorase, LDH, and acid and alkaline phosphatase) in experiments on animals in various periods after infliction of a craniocerebral injury and on autopsy material, i.e. the brain of patients who had died from severe craniocerebral injury incompatible with life. It is shown that the activity of all enzymes decreases (SDH, MDH, NAD-diaphorase, and alkaline phosphatase) or increases (LDH, acid phosphatase) in various periods after the injury. The results were compared with the findings of morphological examination of the same brain areas performed by means of neurohistological methods.
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PMID:[Redox and proteolytic enzymes in brain tissue after a concussion]. 689 60

Tendon tissue of eleven athletes suffering from insertion tendopathy and of two controls was examined. Part of the tissue was prepared for routine light microscopy, a part for enzyme histochemical staining of Nicotinamide-adenine-dinudeotide-diaphorase (NADP-diaphorase), lactate dehydrogenase (LDH), beta-glucuronidase and alkaline phosphatase. Small pieces of tissue were also prepared for electron microscopic examination. The removed tissue was edematous and mushy. The normally densely packed parallel or interwoven collagen bundles were loosened by edema, focal necrosis or hemorrhage. Infiltration of fatty tissue and granulation tissue was also present. The amount of acid mucopolysaccharides was markedly increased. The histochemical studies showed strong enzyme activity of NADP-diaphorase and LDH in normal tendon tissue as well as around areas of degeneration and in granulation tissue. beta-Glucuronidase and alkaline phosphatase was present, but in general with lesser activity than the above enzymes. The electron microscopic examination revealed marked degeneration of the fiber systems, focal necrosis, deposit of amorphous masses and mucopolysaccharides and focal mineralisation. The reparative zones showed proliferating capillaries, often with a collapsed lumen and prominent endothelial cells and basement membranes.
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PMID:Insertion tendopathy in athletes. A light microscopic, histochemical and electron microscopic examination. 712 23

Preparations enriched with plasmalemmal, outer mitochondrial, or Golgi complex membranes from rat liver were subfractionated by isopycnic centrifugation, without or after treatment with digitonin, to establish the subcellular distribution of a variety of enzymes. The typical plasmalemmal enzymes 5'-nucleotidase, alkaline phosphodiesterase I, and alkaline phosphatase were markedly shifted by digitonin toward higher densities in all three preparations. Three glycosyltransferases, highly purified in the Golgi fraction, were moderately shifted by digitonin in both this Golgi complex preparation and the microsomal fraction. The outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the outer mitochondrial membrane marker, monoamine oxidase, was not affected by digitonin in the out mitochondrial membrane preparation, in agreement wit its behavior in microsomes. With the exception of NADH cytochrome c reductase (which was concentrated in the outer mitochondrial membrane preparation), typical microsomal enzymes (glucose-6-phosphatase, esterase, and NADPH cytochrome c reductase) displayed low specific activities in the three preparations; except for part of the glucose-6-phosphatase activity in the plasma membrane preparation, their density distributions were insensitive to digitonin, as they were in microsomes. The influence of digitonin on equilibrium densities was correlated with its morphological effects. Digitonin induced pseudofenestrations in plasma membranes. In Golgi and outer mitochondrial membrane preparations, a few similarly altered membranes were detected in subfractions enriched with 5'-nucleotidase and alkaline phosphodiesterase I. The alterations of Golgi membranes were less obvious and seemingly restricted to some elements in the Golgi preparation. No morphological modification was detected in digitonin-treated outer mitochondrial membranes. These results indicate that each enzyme is associated with the same membrane entity in all membrane preparations and support the view that there is little overlap in the enzymatic equipment of the various types of cytomembranes.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver VIII. Subfractionation of preparations enriched with plasma membranes, outer mitochondrial membranes, or Golgi complex membranes. 725 62

Proximal tubules were isolated in highly pure form from rabbit cortices by a mechanical procedure that is known to preserve the structural and metabolic aspects of the tubular cells. Postnuclear supernates prepared from the isolated tubules were subjects to isopycnic centrifugation in linear sucrose gradients. The enzyme activities associated with the plasma membrane (gamma-glutamyl transpeptidase, amino-peptidase M, alkaline phosphatase, Na-K-ATPase, and phosphodiesterase I) exhibited sharp unimodal frequency-density profiles with a median density near 1.16 g/ml, which shifted to a heavier density when treated with digitonin. The lysosomal enzymes, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and cathepsin B, and the peroxisomal enzyme catalase exhibited particle-associated activity near a density of 1.22 g/ml. Disruption of these particles by freezing and thawing resulted in these activities appearing in the rho = 1.10 g/ml region of the gradient where the soluble cytosolic enzyme, phosphoglucomutase, exhibited activity. Cytochrome oxidase activity typical of mitochondria gave a sharp unimodal profile at rho = 1.18 g/ml. Microsomal glucose-6-phosphatase and NADPH: cytochrome c reductase activities gave median densities near 1.16 g/ml, which did not change after incubation with digitonin. Galactosyl transferase activity gave a skewed profile at rho = 1.16 g/ml and showed a slight shift to heavier density after digitonin. This study of the enzymatic activities and density gradient distribution of the components of the proximal tubule cells provides the methodology for the further study of the cellular processing of endogenous and exogenous substances by this vital cell type.
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PMID:Analytical cell fractionation of isolated rabbit renal proximal tubules. 730 Jan 16

Examination of macrophages, polymorphonuclear leukocytes (PMNL) and lymphocytes of the trachea, PMNL and blood lymphocytes, of the condition of pulmonary tissue in the time course of the process (1st day--l months) revealed an association between the developing cellular and tissue changes. The development of alterations in the lungs with predominant anabolic changes and moderate exudation are characterized by a decrease in the content of nucleoproteins (deoxyribonucleoproteins, ribonucleoproteins), and activity of NAD-diaphorase and alkaline phosphatase, an increase in the activity of acid phosphatase in the above-mentioned cells of the trachea and blood as well as by increased permeability of lysosomal membranes and degeneration of macrophages, PMNL and lymphocytes of the trachea. The above cellular changes in combination with increased permeability of PMNL and blood lymphocyte lysosomal membranes correspond to the development in the lungs of catabolic alterative lesions, marked exudation, and suppurative-necrotic processes. The increase in the content of nucleoproteins and NAD-diaphorase and alkaline phosphatase activity and the decrease in the acid phosphatase activity are accompanied by activation of proliferation in the lungs.
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PMID:[Cyto-histochemical study of morphogenesis of experimental nonspecific pneumonia]. 741 96

The NADPH-diaphorase (NADPH-d) reaction is frequently used to visualize the diaphorase activity of nitric oxide synthase (NOS). However, this tetrazolium salt procedure can be of limited specificity at sites where non-specific alkaline phosphatase (alP) and NADHd activity co-exist. This is shown in the present paper using methods of catalytic histochemistry for these three enzymes and levamisole as alP inhibitor for certain mouse tissues. In the urothelium, portio, vaginal and endometrial epithelium as well as in some smooth muscle cells alP hydrolyzes NADPH to NADH which in turn serves as substrate for NADHd leading to false-positive formazan production. To exclude this possibility, it is recommended always to include levamisole in the incubation medium if the NADPHd activity of NOS has to be investigated.
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PMID:Nonspecific alkaline phosphatase activity can be responsible for staining of NADPH-diaphorase activity in certain non-neural cells. 755 70


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