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)

Twelve acid hydrolases, 4 near-neutral hydrolases, and alkaline phosphatase were demonstrated in 0.34 M sucrose homogenates of Trypanosoma cruzi strain Y: p-nitrophenylphosphatase and alpha-naphthylphosphatase, with optimum pH at approximately 6.0; alpha=ga;actpsodase. beta=ga;actpsodase. beta=g;icpsodase, N-acetyl-beta-glucosaminidase, cathepsin A and peptidase I and III, with optimum pH between 5.0 and 6.0; and arylsulfatase, cathepsin D, alpha-arabinase and alpha-mannosidase with optimum pH at approximately 4.0. alpha-Glucosidase, glucose-6-phosphatase and peptidase II had optimum pH at approximately 7.0. beta-Glycerophosphatase had a broad pH-activity curve from 4,0 to 7.4, with maximum activity at pH 7.0. The main kinetic characteristics of these enzymes and their quantitative assay methods were studied. No activity was detected for alpha-fucosidase, beta-xylosidase, beta-glucuronidase, elaidate esterase, acid lipase, and alkaline phosphodiesterase.
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PMID:Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay. 4 19

The effect of mercury on alkaline phosphatase, lipase, aminotripeptidase and glycylglycine dipeptidase in the liver and digestive tract of Channa punctatus is investigated in vitro. Mercury inhibits the activities of all these enzymes and the degree of inhibition increases with the increase in the concentration of the metal. Addition of EDTA, a chelating agent, restored the mercury inhibited enzyme activity and the degree of restoration was related to the concentration of the chelating agent.
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PMID:In vitro inhibition of digestive enzymes by heavy metals and their reversal by chelating agent: Part I. Mercuric chloride intoxication. 10 87

The effect of lead on alkaline phosphatase, lipase, aminotripeptidase and glycylglycine dipeptidase in the liver and digestive tract of Channa punctatus is investigated in vitro. Mercury inhibits the activities of all these enzymes and the degree of inhibition increased with the increase in the concentration of the metal. Addition of EDTA, a chelating agent, restored the mercury inhibited enzyme activity and the degree of restoration was related to the concentration of the chelating agent.
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PMID:In vitro inhibition of digestive enzymes by heavy metals and their reversal by chelating agent: Part II. Lead nitrate intoxication. 10 88

Scolices and brood capsules of healthy hydatid cysts from lungs of human patients were studied with histochemical and histoenzymatic methods. The subtegumental and flame cells were sepcially rich in glycogen, RNA and some dehydrogenases such as SDH, MDH, NADH-reductase and G-6-PDH. The rostellar zone or invaginated pole, an area of marked contractile movements, showed intense activity in ATP'ase and simple esterase. The so-called excretory pole shows strong activity in simple esterases, lipase, beta-HBH, alpha-GDH and NADPH-reductase. Lipids are also abundant in this zone implying the important role of this metabolic path in the development of the parasite. Intense activity in alkaline phosphatase was observed in cells associated to the calcereous corpuscles. The largest corpuscles were devoid of enzymatic activity. The enzyme could play some role in the calcification of the corpuscles. Wide enzymatic variations are described according to morphology being orthoscolices the most rich in enzyme activity. Accumulations of small cells surrounded by specialized cells on the germinal membrane are interpreted as the origin or "embryo" of brood capsules. Some enzymes detected in the wall of mature brood capsules depicted alternating types of cells. Some of them are positive for ATP'ase that may be related to active transport of substances across the brood capsule wall. The intenst ATP'ase activity at the stalks of scolices may be similarly interpreted. However, a miosine-like activity is a more feasible explanation since this area showed striking contractile movements in vivo.
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PMID:Histochemistry and histoenzymology of the hydatid cyst (Echinococcus granulosus Batsch, 1786). II. Scolices and brood capsules. 13 Jul 50

Rat spermatozoa from the cauda epididymidis, freed from their cytoplasmic droplets and acrosomes, were found to have a lower lipid content and to incorporate [14C]glucose into their glycerides and glycerophosphatides at a lower rate than spermatozoa from the caput epididymidis. Against the background of the activities of some glycolytic enzymes which remained constant the activity of alkaline phosphatase decreased in spermatozoa migrating through the epididymis, whereas the activity of monoglyceride lipase increased. The corresponding enzyme activities of non-flagellate germ cells of the testis were measured for comparison. The triglyceride lipase of non-flagellate germ cells and of spermatozoa from both caput and cauda epididymidis was activated by cyclic 3':5'-AMP.
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PMID:Changes in lipase and phosphatase activities of rat spermatozoa in transit from the caput to the cauda epididymidis. 17 29

Intramuscular administration of cortisone acetate (5 mg daily to each for 15 days) to adult male pigeons provoked hypertrophy of the preen gland. Desquamation and loss of alveolar differentiated cells were also accelerated to a great extent. Significant changes observed in the histochemical composition of the alveoli of the preen gland of cortisone-treated pigeons were: (a) a greater accumulation of sudanophilic lipids within the alveoli, (b) an increase in the content of acidic lipids, (c) a decrease in the activity of acid phosphatase, and (d) an overall augmentation of the reaction for alkaline phosphatase. There was, however, no gross change in the activities of nonspecific esterases and lipase. The probable significance of the cortisone-induced glandular hypertrophy and histochemical changes has been briefly discussed.
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PMID:Histomorphological and histochemical studies on the preen gland of cortisone-treated male pigeons. 18 24

The effect of LC(50) and a sublethal concentration of lead nitrate on the activities of alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, lipase and urease in the kidneys and ovaries of a teleost fish, Channa punctatus has been examined after 96 hr and 30 days respectively. The results show that all the five enzymes in the two tissues are inhibited significantly at both the experimental stages. However, the inhibition produced after 30 days by the sublethal concentration ish higher indicating the cumulative action of lead. Further, the inhibition of enzymes is, more marked in kidney than in the ovary.
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PMID:Effects of lead nitrate on the activities of a few enzymes in the kidney and ovary Heteropneustes fossillis. 22

Acid-and alkaline phosphatase, 5-nucleotidase and lipase have been localized histochemically in the gizzard, intestine liver and pancreas of Indian parrot, Psittacula krameri. In the gizzard and intestine, the mucosal epithelial cells are the main sites for the enzyme production. The tubular glands of the gizzard show intense reaction for all the enzymes tested. The hepatic sinusoid cells of the liver and the acinii of pancreas give positive reaction. Like pancreas, the intestine has also been found responsible for the production and secretion of lipase. Functional significance of phosphatases in the tissues tested has been discussed.
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PMID:Histochemical study of the distribution of a few enzymes in the digestive system of Indian parrot. 40 19

Mutants of Pseudomonas aeruginosa strain PAKS-I which are defective in the formation of extracellular protease activity have been characterized. The mutants produced between approximately 1 and 25% of the protease activity of the wild type and no strains completely lacking extracellular protease were found, even after repeated mutagen treatment. Most mutants also had changed activities of extracellular staphylolytic enzyme, lipase and lecithinase. Four of 13 mutants were unable to release alkaline phosphatase and staphylolytic enzyme into the medium in contrast to the wild type. Serotype, phage type and biochemical reactions were essentially unchanged. The results indicate that some of the mutations affected the cell envelope structure of function leading to decreased ability to release extracellular proteins, and that other mutations possibly affected a common regulatory mechanism for extracellular enzymes.
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PMID:Protease-deficient mutants of Pseudomonas aeruginosa: pleiotropic changes in activity of other extracellular enzymes. 41 77

The activity of amylase, alkaline phosphatase and lipase in the pancreas, in the mucosa and on the surface of small intestine (turned out segments) was studied for elucidating the effect of vitamin A deficiency on the synthesis of the studied enzymes and their translocation to the surface of glycocalix cell membranes. The activity of amylase is established to increase in the homogenate of the pancreas, intestine mucosa and on the surface of cell membranes. The activity of alkaline phosphatase and lipase in the homogenate of small intestine mucosa and in the pancreas lowers. The results obtained evidence for a disturbance in the intestine digestive function with vitamin A deficiency, the may be connected with the damage of the mucosa membrane structures as well as with a disturbance in the biosynthesis of the protein playing a decisive role in formation of secretory products in cells.
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PMID:[Study of hydrolase activity of rat small intestine mucosa with vitamin A deficiency]. 72 94


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