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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 immunochemical and structural characteristics of the alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] from mouse teratoma stem cells derived from the OTT-6050 teratoma (ascitic and solid tumors and the F9 and PCC4 cell lines) have been compared to those of the alkaline phosphatases expressed in normal mouse placenta and several adult organs. Crossreactivity of the stem cell alkaline phosphatase with antisera reacting with placental, kidney, liver, and brain alkaline phosphatases indicated that the stem cell enzyme had common antigenic determinants. Structural studies utilizing two-dimensional electrophoresis of the (32)P-labeled alkaline phosphatase subunits showed that the stem cell, placental, and kidney alkaline phosphatases differed only in their sialic acid content and comigrated after removal of terminal sialic acid by neuraminidase digestion. Furthermore, one-dimensional peptide mapping of partial proteolysis fragments from (32)P-labeled enzymes demonstrated identical fragmentation patterns for the stem cell and somatic enzymes. These immunochemical and structural data indicate that the stem cell alkaline phosphatase is the same core enzyme as that produced in the mouse placenta and kidney, with different amounts of terminal sialic acid. The one mouse alkaline phosphatase examined that differed from the other enzymes was the intestinal alkaline phosphatase. This isoenzyme was not immunochemically crossreactive with the other alkaline phosphatases, did not comigrate in two-dimensional electrophoresis after neuraminidase digestion, and did not give identical peptide maps after partial proteolysis.
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PMID:Alkaline phosphatase of mouse teratoma stem cells: immunochemical and structural evidence for its identity as a somatic gene product. 28 2

Alkaline phosphatases [ALPases; orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] from dog and human placenta, liver, bone, kidney, and intestine were investigated by inhibition studies with L-homoarginine, L-phenylalanine, and L-phenylalanylglycyl-glycine; by thermostability studies; and by electrophoresis, both before and after treatment with neuraminidase. The inhibitions obtained for each inhibitor with dog placental ALPase closely match those obtained with dog and human liver, bone, and kidney ALPases, but are quite different from those obtained with human placental ALPase. Dog placental ALPase is thermolabile, as are dog and human liver, bone, and kidney ALPases, in marked contrast to human placental ALPase, which is very thermostable. Dog placental ALPase has the same electrophoretic mobility as dog liver, bone, and kidney ALPases after removal of sialic acid residues with neuraminidase. Desialated human placental ALPase differs electrophoretically from desialated human liver, bone, and kidney ALPases, which show the same mobilities. Dog and human intestinal ALPases are distinguished by these various criteria from the liver, bone, kidney, and placental ALPases of both species, but are similar to each other. These results suggest that the ALPase gene locus expressed in dog placenta is not homologous to that expressed in human placenta. Rather, it appears to be homologous to the ALPase locus expressed in dog and human liver and possibly also bone and kidney. Other incomplete data suggest that this may also be true for placental ALPase in other mammalian species. One possible explanation is that human placental ALPase, a relatively recent newcomer on the evolutionary scene, arose from a gene duplication that occurred subsequent to the evolutionary divergence of many other mammalian species.
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PMID:Lack of homology between dog and human placental alkaline phosphatases. 28 36

Sera from 8 patients with a marked slow-moving alkaline phosphatase band on electrophoresis were investigated. Inhibitor studies and treatment with neuraminidase showed that all the patients had slow bands with alkaline phosphatase properties resembling those of the liver or bone isoenzyme. In no case did the slow band resemble the intestinal isoenzyme. Immunoelectrophoretic and molecular weight studies indicated that the slow band consisted of an IgG-alkaline phosphatase complex of molecular weight 540 000. Serum from a patient with the slow band was able to bind liver or bone, but not intestinal, alkaline phosphatase from other patients to form the slow band. Serum from patients with the slow band probably contains an abnormal IgG molecule which can bind alkaline phosphatase in the ratio 2:1. No clinical condition was common to all 8 patients although most of them had either intestinal or lung disease.
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PMID:The properties and clinical significance of some electrophoretically slow forms of alkaline phosphatase. 30 71

The origin of canine serum alkaline phosphatase (ALP) was investigated by various means. On the basis of electrophoretic migration, neuraminidase treatment, thermal denaturation, and chromatographic fractionation, canine serum was found to contain ALP principally of hepatic origin. There was evidence of only a minor portion of ALP being of osseous origin. Intestinal ALP was not detected in canine serum when monitored by immunochemical technique, L-phenylalanine inhibition, and thermal denaturation.
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PMID:Origin of serum alkaline phosphatase in the dog. 35 72

Sera of several canine patients contained an isoenzyme of alkaline phosphatase (ALP) that resembled intestinal ALP with respect to heat inactivation, L-phenylalanine inhibition, and sensitivity to anti-canine intestinal ALP antibody, but differed with regard to the electrophoretic migration. The electrophoretic mobility of the isoenzyme was slightly cathodal than that of hepatic ALP, and its migration was reduced, similar to that of hepatic isoenzyme after neuraminidase treatment. This isoenzyme, which could be corticosteroid induced, was in the sera of numerous dogs with hepatobiliary disorders and was different from the hepatic isoenzyme that appeared in the sera of dogs with acute hepatitis, based on anti-canine intestinal ALP antibody interaction, heat inactivation, and electrophoretic migration.
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PMID:Diagnostic evaluation of canine serum alkaline phosphatase by immunochemical means and interpretation of results. 35 73

Using fresh frozen, freeze-dried or cryostate sections from aldehyde fixed rat tissues 13 diazonium salts were tested as simultaneous coupling reagents for the localization of acid, neutral and alkaline hydrolases with azo indoxyl methods. Hexazotized new fuchsine and/or Fast blue B are the diazonium salts of choice for the demonstration of acid beta-galactosidase, neuraminidase, beta-N-acetylglucosaminidase, acid phosphatase, and non-specific esterase followed by hexazotized p-rosaniline. Fast blue VB, BB and RR and Fast violet B are recommended for the investigation of alkaline phosphatase and lactase, Fast garnet GBC for acid beta-galactosidase, glucosaminidase and lactase. Fast red B, RC, RL and TR and Fast black K can only be employed for lactase studies. The exact concentration of the coupling reagent depends on the activity of the enzyme and the organ imvestigated. On the average 0.01-0.02 ml unstable diazonium salt/ml and 0.3--1 microgram stable diazonium salt/ml are sufficient for the correct localization of these hydrolases. Freeze-dried cryostat sections yield the best results in the demonstration of lactase and alkaline phosphatase independent on the coupling reagent used. Sections from formaldehyde or glutaraldehyde fixed organs are superior for the localization of the other hydrolases; an exception is the investigation of acid beta-galactosidase and glucosaminidase with Fast garnet GBC. Then, excellent results are obtained also with freeze-dried material. Fresh frozen sections are suitable for the localization of lactase with hexazotized new fuchsine or p-rosaniline and of alkaline phosphatase with Fast blue VB and BB or violet B. The total activity of acid, neutral and alkaline hydrolases can be investigated using semipermeable membranes in combination with all unstable and stable diazonium salts of choice. Reliable osmification of the azoindoxyl dye is only possible if hexazotized p-rosaniline is employed for coupling; without further posttreatment all azoindoxyl dyes are extracted by ethanol, isopropanol or xylol. 7 incubation media are given for the demonstration of hydrolases with azoindoxyl methods at the level of light microscopy for routine studies and typical examples for the application of these methods are presented. A modified procedure is described for the freeze-drying of cryostat sections with the Edwards-Pearse tissue dryer EPD3.
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PMID:[Azoindoxyl methods for the investigation of hydrolases. IV. Suitability of various diazonium salts (author's transl)]. 36 63

Lysosomal hydrolases in fibroblasts and leucocytes exhibited the same isoelectric focusing pattern as found in liver. Treatment with neuraminidase had a great effect on the pattern of several glycosidases while treatment with alkaline phosphatase did not significantly change the pattern. These findings are discussed with special reference to the different "uptake" systems that exist for acid hydrolases.
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PMID:Isoelectric focusing of acid hydrolases in human fibroblasts and leucocytes. 44 42

Genetic variation among inbred strains is described for electrophoretic migration of alkaline phosphatase from intestine, kidney, blood plasma, and three isozymes of liver. A manganese-requiring isozyme of liver and kidney unaffected by neuraminidase is described, and the locus controlling variation in this isozyme is designated Akp-1. Data from recombinant inbred strains place the locus on chromosome 1 at a distance of 3.6 +/- 2.9 cM from the M1s locus on the side distal to the centromere. Test-cross data show the following gene order and recombination percentages: Dip-1 19.0 +/- 3.8% Lp 7.4 +/- 2.2% Akp-1.
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PMID:Genetic variation in alkaline phosphatase of the house mouse (Mus musculus) with emphasis on a manganese-requiring isozyme. 54 2

Lectins from Canavalia ensiformis, Phaseolus vulgaris, and Triticum vulgare react with arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase of human sera by formation of enzymatically active, mostly insoluble complexes. Arylamidase, alkaline phosphatase, and cholinesterase react more intensely in sera of healthy people than in sera of patients with liver and neoplastic diseases. Arylesterase is bound to a distinct degree only by concanavalin A. The enzymes mentioned above also react slightly with the following lectins in order of decreasing intensity: Ricinus communis, Arachis hypogaea, Helix pomatia, Glycine max, Dolichos biflorus, and Ulex europaeus. Though multiple forms containing less sialic acid are favourably bound, preincubation with neuraminidase does not improve the reaction except with soybean lectin. Since higher concentrations of lectins react also with fast moving fractions of high sialic acid content, no steric hindrance of the binding between lectins and sialoenzymes is supposed, as concluded from determination of the total enzyme activity.
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PMID:[Lectins as reagents for the differentiation of serum enzymes. Lectins as reagents, I. (author's transl)]. 54 35

In electron microscope cytochemical studies alkaline phosphatase activity was present in the mitochondria of all liver cells and associated with the plasma membrane of the cells of bile canaliculi. The mitochondrial activity was partially inhibited by L-phenylalanine and Levamisole but the plasma membrane associated activity was completely inhibited by Levamisole. Biochemical assays have shown that a significant amount of the total mouse liver alkaline phosphatase activity was present in the mitochondria fraction. Starch gel electrophoresis showed that this mitochondrial alkaline phosphatase had a characteristic isoenzyme pattern, consisting of 3 distinct bands which were not retarded by neuraminidase treatment. The enzyme in the mitochondria-free supernatant showed one wide band which was retarded by neuraminidase.
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PMID:Alkaline phosphatase in mitochondria. 61 Aug 69


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