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)

Hormone-induced alkaline phosphatases in human osteosarcoma cells (LM) were extracted and purified. Characterization of the purified enzyme showed two distinct isoenzymes. One isoenzyme was heat labile, was homoarginine inhibited, and had the electrophoretic migration of alkaline phosphatase of human osseous origin. Immunodiffusion showed that this isoenzyme reacted positively only against anti-bone alkaline phosphatase antibodies. The second isoenzyme was heat stable, was inhibited by phenylalanie, and had the same electrophoretic migration as did alkaline phosphatase extracted from mature normal human placenta. This second isoenzyme had the same antigenicity as did the normal placental enzyme. Like the D-variant placental phenotype, this second isoenzyme was inhibited by L-leucine and ethylenediaminetetraacetic acid.
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PMID:Placenta-like alkaline phosphatases from human osteosarcoma cells. 2 98

Two cases of liver metastases from gastric carcinoma are described in which the simultaneous occurrences of alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA) and carcinoplacental alkaline phosphatase (CPALP) were demonstrated in the sera and tumor tissues. AFP was detected not only in the tumor tissues but also in the liver tissue adjacent to the tumor, while the other 2 carcinoembryonic proteins were not detected in the non cancerous liver tissues. The characteristics of CPALP in Case 1 were almost similar to the Nagao isoenzyme, based on enzyme tests involving L-leucine, L-phenylalanine and EDTA inhibitions, heat-stability and Michaelis constant, except for electrophoretical slower moving, while that in Case 2 were identical to variant type CPALP (Warnock).
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PMID:Carcinoembryonic proteins in gastric carcinoma metastatic to the liver. 9 60

Another Kasahara-variant alkaline phosphatase isoenzyme was found in 2 out of 25 human renal cell carcinoma tissues. This enzyme electrophoresed in a single diffuse band which is cathodal to but continuous with the liver alkaline phosphatase. After neuraminidase treatment, this enzyme electrophoresed in the same position as that of neuraminidase-treated Kasahara isoenzyme. The enzymic properties of another neuraminidase-treated Kasahara-variant enzyme such as inhibitions by L-phenylalanine, L-homoarginine, L-tryptophan, and L-leucine, effects of inorganic phosphate, urea, and sodium dodecyl sulfate, heat stability, and the reactivity with concanavalin-A are consistent with those of Kasahara isoenzyme. On Ouchterlony's double diffusion, the precipitin lines of Kasahara and the new variant enzyme produced by antibody to Kasahara isoenzyme fused completely. These facts may indicate the occurrence of another Kasahara-variant isoenzyme.
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PMID:Another Kasahara-variant alkaline phosphatase in renal cell carcinomas. 11 99

Lactoperoxidase-catalysed iodination was used to label intestinal epithelial cell sheets with 125I. The iodination was carried out under conditions that allowed little penetration of lactoperoxidase into the cells and membrane-bound 125I therefore provided an effective marker for following plasma-membrane fragments through subcellular-fractionation procedures. 2. After homogenization and isopycnic zonal centrifugation through sucrose gradients two peaks of membrane-bound 125I were detected. One coincided with brush border enzymes such as alkaline phosphatase, disaccharidases and L-leucine B-naphthylamidase, whereas the other was coincident with the major peak of (Na++K+)-stimulated ATPase (adenosine triphosphatase), which has been thought to be concentrated in the basolateral plasma membranes of these cells. Neither peak of 125I reflected the distribution of any marker for an intracellular organelle. 3. A larger proportion of the (Na++K+)-stimulated ATPase, and thus of the basolateral plasma-membrane material, was found in a crude 'mitochondrial' fraction. It was not readiily separated from mitochondria by conventional techniques of subcellular fractionation. 4. Treatment of the 'mitochondrial' fraction with digitonin increased the density of basolateral plasma membrane but had little effect on mitochondrial density. A purified preparation of digitonin-loaded basolateral plasma membranes was isolated at a density of 1.20-1.22 by isopycnic centrifugation. 5. The enzymic composition of this preparation of basolateral plasma membranes is compared with previous preparations isolated from intestinal mucosal 'scrape' materials and from isolated cells.
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PMID:Basolateral plasma membranes of intestinal epithelial cells. Identification by lactoperoxidase-catalysed iodination and isolation after density perturbation with digitonin. 12 58

Electrophoretically Kasahara-variant alkaline phosphatase we found in a renal cell carcinoma tissue. This enzyme electrophoresed more quickly than liver alkaline phosphatase but more slowly than Kasahara isoenzyme. Neuraminidase treatment of the enzyme caused retardation of electrophoretic mobility which was the same as that of neuraminidase-treated Kasahara isoenzyme. The enzymic properties of this variant enzyme such as inhibition by L-phenylalanine, L-homoarginine, L-leucine, EDTA and urea are consistent with those of Kasahara isoenzyme. On Ouchterlony double diffusion, the precipitin lines of Kasahara and Kasahara-variant enzymes produced by antibody to Kasahara isoenzyme fused completely. These facts may mean that Kasahara-variant isoenzyme is different from the Kasahara one in terminal sialic acid content.
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PMID:Kasahara-variant alkaline phosphatase in a renal cell carcinoma. 21 14

Starch gel electrophoresis and inhibition studies with L-phenylalanine, L-homoarginine, L-leucine, L-leucylglycylglycine, and L-phenylalanylglycylglycine were carried out on a series of human alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] derived from fetal and adult liver, kidney, bone, and intestine. No differences between adult and fetal liver, kidney, or bone alkaline phosphatases were observed by either electrophoretic or inhibition studies. However, the fetal intestinal enzyme could be clearly distinguished from the adult intestinal enzyme by its greater anodal electrophoretic mobility and its retardation after treatment with neuraminidase. Even after extensive neuraminidase treatment, its anodal mobility was still slightly greater than that of adult intestinal alkaline phosphatase. Fetal and adult intestinal enzymes showed the same inhibition profiles with the series of inhibitors both before and after treatment with neuraminidase. A survey of intestinal samples from fetuses and premature infants of various gestational ages indicated that the changeover from the synthesis of fetal to adult intestinal enzyme begins at about 28-32 weeks of gestation. The difference between the fetal and adult forms of intestinal alkaline phosphatase may represent the expression of different gene loci or a difference in post-translational modification.
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PMID:Developmental change in human intestinal alkaline phosphatase. 27 6

A fast-moving alkaline phosphatase band on polyacrylamide gel electrophoresis has been found in 6 patients with carcinoma of the liver and gastrointestinal tract. This isoenzyme resembled the placental isoenzyme in its inhibition by L-phenylalanine, its resistance to L-homoarginine inhibition and its molecular weight. However, it differed from the placental and Regan isoenzymes in its sensitivity to L-leucine and ethylenediaminetetra-acetic acid, its lower retardation by neuraminidase, its electrophoretic mobility and its decreased heat stability. The latter two properties also distinguished it from the Nagao isoenzyme. It was identified as the Regan Variant. The Regan Variant has hitherto been reported largely in hepatocellular carcinoma. In the presented paper we report its appearance in the sera of patients who have neoplasms in a variety of primary sites in the gastrointestinal tract. It is emphasized that, while the presence of the Regan Variant in serum may be taken as evidence of carcinoma, no conclusions can be drawn as to the site of the disease.
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PMID:Regan variant alkaline phosphatase in gastrointestinal carcinoma. 65 33

1. The hydrolysis of glycyl-L-leucine, glycyl-L-tyrosine, tributyrin, sucrose, maltose, soluble starch and alpha- and beta-glycerophosphates by everted segments of rat intestine was estimated separately or in combination. 2. A comparative study showed significant interaction between different substrates which affected their digestion. 3. Two types of interaction were identified: products of hydrolysis (1) affected the hydrolysis of homologous substances, e.g. methionine and alanine inhibited glycyl-L-leucine hydrolysis, maltose reduced glucoamylase (alpha-1,4-glucan glucohydrolase; EC 3-2-1-3) activity (intracatenary interactions); (2) interfered with the hydrolysis of a different group of substances, e.g. tributyrin inhibited dipeptidase (glycyl-L-leucine hydrolase; EC 3-4-3-2) and alkaline phosphatase (EC 3-1-3-1), glycyl-L-leucine interfered with the activity of the latter enzyme (intercatenary interactions). 4. Mechanisms of interactions were suggested by the results of a comparison of the extent of inhibition or activation of two enzymes (glycyl-L-leucine hydrolase and alkaline phosphatase) in situ in everted intestinal segments or after solubilization with papain or Triton X-100, and different treatments known to affect allosteric sites of these enzymes. 5. Tributyrin and dipeptides were found to act on alkaline phosphatase as allosteric regulators. A discontinuity of the Arrhenius plot suggested the existence of different enzyme conformations which were re-arranged by tributyrin. 6. Substrate interactions in digestion were found in adult rat, cat, rabbit and hen. Substantial differences were found between classes (Aves and Mammalia), orders (rodents, lagomorphs and carnivores) and between age-groups within an animal strain (in this instance, for the rat). 7. These interactions are thought to be involved in the co-ordination of digestion with intestinal absorption and to regulate the time and site of subsequent hydrolysis.
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PMID:Substrate interactions on the intestinal mucosa: a concept for the regulation of intestinal digestion. 117 95

The effects of divalent cations and of some inhibitors on the activities of alkaline phosphatase and ATPase were examined in rat jejunal brush-border membranes (BBM) isolated by tha Ca(2+)-(BBMCa) or the Mg(2+)-precipitation method (BBMMg). Similar results were found in BBMCa and BBMMg though generally higher in BBMCa. Alkaline phosphatase activity was stimulated by 5 mM MgCl2 (30% to 44%), but not by 5 mM CaCl2 or 0.1 mM ZnCl2, at pH 9.5 or 7.4. ATPase activity was equally stimulated by 5 mM MgCl2 and by 5 mM CaCI2 (about 150%). Alkaline phosphatase activity was significantly inhibited by 1 mM vanadate, 5 mM diamox, 5.0 mM L-leucine and 1 mM theophylline. In contrast, Ca(2+)-ATPase and Mg(2+)-ATPase activities were not depressed by those alkaline phosphatase inhibitors, but were inhibited by 0.1 mM trifluoperazine (more than 70%). 0.1 mM ZnCl2 also appeared to be inhibitory to Ca(2+)-ATPase and Mg(2+)-ATPase, but not to alkaline phosphatase activity even in the presence of Ca2+ and Mg2+. These results suggest that Ca(2+)-ATPase and Mg(2+)-ATPase activities of the rat jejunal BBM are not merely manifestations of alkaline phosphatase, but rather belong to (a) distinct enzyme(s).
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PMID:Alkaline phosphatase and ATPases in brush-border membranes of rat jejunum: distinct effects of divalent cations and of some inhibitors. 138 82

Metronidazole (Flagyl), an antibiotic commonly used in treating intestinal infections, when administered orally at a dose level of 100 mg/kg body weight daily for 7 days to rats brought about a significant elevation of the uptake of end-product nutrients like D-glucose, L-alanine, L-aspartic acid and L-leucine in the intestinal segments. Brush border membrane-bound hydrolytic enzymes, i.e. sucrase, lactase, maltase, alkaline phosphatase and leucine aminopeptidase levels, were also elevated. Substrate kinetic analysis of the uptake of nutrients as well as the enzymes indicated that the drug increased the maximum of apparent initial velocity, while the substrate affinity constants did not change. Studies of the temperature-dependent parameters of the nutrient uptake and the enzyme activity revealed that metronidazole did not induce any shift in the transition temperature (T(o)) for the uptake but the energy of activation (Ea) was reduced in all the cases except those of maltase and leucine aminopeptidase, which registered an increase in Ea and a marginal shift in T(o), respectively. A significant elevation was seen in the levels of membrane cholesterol, phospholipid, ganglioside and plasmalogen in metronidazole-treated animals, while triglycerides and the non-esterified fatty acids remained unaffected. The effects produced by metronidazole treatment persisted in the animals, which were allowed a recovery period of 7 days after the drug regimen.
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PMID:Effect of the antiprotozoal agent metronidazole (Flagyl) on absorptive and digestive functions of the rat intestine. 147 60


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