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)

1. The effect of lipolytic, glycolytic and proteolytic enzymes on the activities of plasma membrane enzyme activities in rat liver and kidney has been investigated by a pretreatment of tissue sections with the lytic enzymes. 2. The action of the proteolytic enzymes causes a very strong decrease of leucyl-beta-naphthylamidase activity, whereas the activities of ATP-ase, 5'-nucleotidase and alkaline phosphatase show a lesser decrease. This indicates a different membrane anchorage of leucyl-beta-naphthylamidase as compared to that of the phosphatases. 3. Treatment with glycolytic enzymes results in a decrease of 5'-nucleotidase and ATP-ase activity, whereas liver alkaline phosphatase and leucyl-beta-naphthylamidase show an increase in activity. 4. Treatment with phospholipase C gives about the same results. The very strong decrease of 5'-nucleotidase activity indicates a great dependence on phospholipids.
Histochemistry 1978 Dec 01
PMID:A histochemical study about the influence of lytic enzymes on plasma membrane enzyme activities in rat liver and kidney. 10 67

Using freeze-dried or sections from fresh-frozen or aldehyde-fixed material nitro BT (NBT), tetranito BT (TNBT), distyryl nitro BT (DS-NBT), thiocarbamyl nitro BT (TC-NBT) or benzothiazolylstyrylphthalhydrazidyl tetrazolium chloride (BSPT) were tested as auxiliary reagents for the localization of glycosidases, phosphatases and non-specific esterases with indoxyl substrates in rat tissues. By means of NBT or TNBT as a tetrazolium salt acid beta-D-galactosidase, beta-D-N-acetylglucosaminidase, acid phosphatase, neuraminidase and non-specific esterase can only be localized at the cellular level; a more precise localization is possible for lactase-beta-D-glucosidase in the intestinal brush border, and the best results are obtained in the demonstration of alkaline phosphatase; among all methods described previously the tetrazolium procedure with TNBT is the method of choice for the light microscopic localization of this enzyme. Reverse data are observed with BSPT as a tetrazolium salt; then, all acid and neutral hydrolases can be exactly localized in lysosomes, secretion granules, cytoplasm and/or microvilli of many cells and tissues provided BSPT-formazan is stabilized by osmification. Furthermore, this procedure enables the reliable ultracytochemical demonstration of these enzymes. However, in the case of alkaline phosphatase only sites with high enzyme activity reveal a positive reaction. -DS- and TC-NBT are inferior to NBT, TNBT or BSPT.
Histochemistry 1978 Dec 01
PMID:[Tetrazolium methods for the histochemical investigation of hydrolases (author's transl)]. 10 69

Liver enzymes alkaline phosphatase and transaminases (GPT & GOT) were studied in cases of protein-depleted rats. Alkaline phosphatase activities were determined with and without Mg addition to the incumedia, since it is the essential metal for this enzyme. The liver transaminases were also determined before and after pyridoxine injection, which is the coenzyme for this group. Both liver alkaline phosphatase and transaminases activities were increased on protein depletion. The study indicates that the increased activities of liver alkaline phosphatase in protein-depleted animals is suggestive of increased enzyme protein synthesis. On the contrary, high activities of liver transaminases are suggestive to be a result of some regulation mechanisms between the enzyme protein and its coenzyme.
Z Ernahrungswiss 1978 Dec
PMID:Some aspects on liver enzymes in protein-energy malnutrition. 10 56

Intestinal mucosa from 40 patients obtained by fiber-endoscopic biopsy was assayed for disaccharidases to determine suitability of this tissue for assay. The combined specimens from each patient provided 4.7-38.7 mg of tissue, adequate in all instances for duplicate determinations of protein, lactase, sucrase, and maltase. Tissue remained for assays of palatinase in 39 instances, trehalase and cellobiase in 37, and alkaline phosphatase in 22 cases. Twenty-four subjects had normal lactose tolerance tests and normal sucrase/lactase ratios. Thirteen patients with abnormal oral lactose tolerance tests were identified as having a primary low lactase activity on the basis of elevated sucrase/lactase ratios. This ratio was most helpful in making the diagnosis of a primary low lactase, since the mucosal specimens were not obtained from comparable areas. Tissue from three subjects with an abnormally low maltase was unsuitable for diagnosis. Endoscopic biopsy of mucosa appears to be satisfactory for disaccharidase assays in most instances.
Am J Dig Dis 1978 Dec
PMID:Adequacy of endoscopic biopsy specimens for disaccharidase assays. 10 20

A significant correlation between the activity of the bone isoenzyme or serum alkaline phosphatase and the urinary hydroxyproline excretion in osteomalacia, osteoporosis, primary hyperparathyroidism with osteodystrophy, Paget's disease, secondary bone tumours, and in a control group was found (P less than 0.001). This close correlation was not observed between these variables in patients with active acromegaly. Diagnosis determined from these indices of formation and turnover of bone matrix agreed with that established by histological and histochemical examination of bone, by X-ray investigation of the skeleton, and by the radionuclear 85Sr test. The relationship between the activity of bone isoenzyme and urinary hydroxyproline excretion differed in metabolic bone diseases with a high bone turnover, in patients with osteoporosis and in patients with early osteoclastic bone metastases.
Eur J Clin Invest 1978 Dec
PMID:Relationship of the activity of the bone isoenzyme of serum alkaline phosphatase to urinary hydroxyproline excretion in metabolic and neoplastic bone diseases. 10 9

Grivet monkeys infected with virulent Francisella tularensis Strain Schu S4 showed significant early changes in serum levels of trace metals, triglycerides and activities of alkaline phosphatase, lactate dehydrogenase and alpha-hydroxybutyrate dehydrogenase. Free amino acid levels decreased slightly and there was a marked increase in the phenylalanine: tyrosine ratio. Serum lysozyme activity and seromucoid levels also increased. Kanamycin therapy produced remission of overt signs but the changes in blood constituents were less readily affected. Immunization with the live vaccine strain of F. tularensis induced transient responses similar to those resulting from Schut S4 infection. Immunized monkeys subsequently challenged with the virulent Schu S4 strain showed no clinical signs or marked changes in blood constituents.
Br J Exp Pathol 1978 Dec
PMID:Changes in whole blood and serum components of grivet monkeys with experimental respiratory Francisella tularensis infection. 10 70

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.
Bull Environ Contam Toxicol 1978 Dec
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.
Bull Environ Contam Toxicol 1978 Dec
PMID:In vitro inhibition of digestive enzymes by heavy metals and their reversal by chelating agent: Part II. Lead nitrate intoxication. 10 88

Cultures of Bacillus subtilis were treated during sporulation with antibiotics (bacitracin and vancomycin) that affect peptidoglycan synthesis. The cells were resistant to the effects of the antibiotics only when the drugs were added about 2 h after the beginning of sporulation. This was about 1 h later than the escape time of a temperature-sensitive sporulation mutant that is unable to complete prespore septation. Similar experiments were done with a mutant temperature sensitive for peptidoglycan synthesis. This showed an escape curve similar to that shown by the antibiotics. When sporulating cells were treated with antibiotics, they produced alkaline phosphatase earlier than normal. Enzyme production was unaffected by inhibition of deoxyribonucleic acid synthesis but was inhibited by chloramphenicol. Sporulation mutants that are unable to make alkaline phosphatase under normal conditions were able to make it in the presence of bacitracin. The alkaline phosphatase made under these conditions was under "sporulation-type" control since its synthesis was repressible by casein hydrolysate and unaffected by inorganic phosphate. When cells were treated with bacitracin in the growth medium as well as in the sporulation medium, alkaline phosphatase synthesis was at the same level as in an untreated control. A number of other antibiotics and surfactants were tested for the ability to cause premature production of the phosphatase of those tested, only taurodeoxycholate whowed this behavior. Moreover, incubation of cells with taurodeoxycholate in the growth medium as well as in the sporulation medium prevented premature enzyme production.
J Bacteriol 1979 Dec
PMID:Requirement for peptidoglycan synthesis during sporulation of Bacillus subtilis. 11 56

During the activation of the inactive dinitrogenase reductase from Rhodospirillum rubrum, an adenine-like molecules is lost and phosphate is found on both active and inactive forms of the protein. ATP and divalent metals are required for activation of the reduced protein, but ATP is not required for activation of phenazine methosulfate-oxidized dinitrogenase reductase. Snake venom diesterase and spleen diesterase have no effect on the inactive protein; alkaline phosphatase removes phosphate from the activated protein but not from the inactive protein. ATP binds to both active and inactive forms of the protein.
Proc Natl Acad Sci U S A 1979 Dec
PMID:Removal of an adenine-like molecule during activation of dinitrogenase reductase from Rhodospirillum rubrum. 11 62


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