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 proportions of the total activities of different isoenzymes of human alkaline phosphatase precipitated from serum by ethanol (20% v/v) were: liver phosphatase, 37%; placental phosphatase, 23%; bone phosphatase, 8.0%, and small-intestinal phosphatase, 3.7%. Treatment of the isoenzymes with neuraminidase reduced the percentages of non-intestinal phosphatases precipitated by ethanol to below 10%. Precipitation of intestinal alkaline phosphatase was unaffected by this treatment. The degree of solubility in ethanol therefore appears to be largely determined by the content of terminal sialic acid residues in the alkaline phosphatase molecules. In contrast the stabilities of the isoenzymes to heating at 56 degrees C were not significantly altered by neuraminidase digestion.
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PMID:Further observations on the differential precipitation of alkaline phosphatase isoenzymes by ethanol. 62 Apr 61

Alkaline phosphatase activity of rat serum was reduced 50% by fasting the animal for 24 hours. Diabetes, induced by alloxan or streptozotocin, increased serum alkaline phosphatase 3- to 5-fold in fed rats and the elevated activity was reduced by insulin administration. In the absence of insulin, fasting alone was able to reduce the serum alkaline phosphatase of diabetic rats to control values. The elevated serum isozyme was found to be of intestinal origin by the use of appropriate inhibitors and electrophoretic mobility following neuraminidase treatment. It is concluded that food intake, particularly the hyperphagia of diabetes, plays a major role in regulating the concentration of intestine and serum alkaline phosphatase in the rat.
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PMID:Effects of experimental diabetes and food intake on rat intestine and serum alkaline phosphatase. 62 74

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

A close correlation between the intensity of tissue reaction in skeletal muscles and the localization of some enzymes in the bladder of C. bovis was demonstrated by histochemical methods. The most intensive tissue reaction was observed around the portion of bladder surrounding the opening of spiral canal, the tegument and subtegumental cells of which exhibit a high activity of alkaline phosphatase and acid phosphatase. Around this portion of bladder the tissue reaction is very strong, whereas around the remaining portion of the bladder, without any activity of these enzymes, the reaction is weak. The basic type of the reaction around the portion with alkaline and acid phosphatase activity is the formation of a pseudoepithelial rim, in which occur secondary changes leading to histochemical changes inside and around this rim. The cells of the unchanged pseudoepithelial rim contain proteins with tyrosine, tryptophan and cysteine. Among the cells is a large number of reticular fibres. Flat foci localized directly in this rim contain mostly fibrilar structures rich in acid mucosubstances with carboxyl and sulphate groups which are labile to testicular hyaluronidase and neuraminidase. They contain also a small amount of neutral mucosubstances and give negative reactions for tyrosine, tryptophan and cysteine. Fibrilar structure in these foci undergo dystrophic calcification. A conspicuous accumulation of mast cells is visible in the layers under the pseudoepithelial rim and clusters of cells containing lipopigment are present at the periphery of the connective tissue layer.
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PMID:Histochemistry of tissue reaction in skeletal muscles of cattle experimentally infected with Cysticercus bovis. 74 48

Alkaline phosphatase from human and calf small intestines has been prepared and purified until homogeneous, as judged by polyacrylamide gel electrophoresis, by means of the following techniques: n-butanol extraction, ammonium sulfate precipitation, acetone fractionation, ion exchange chromatography and isoelectric focusing in a sucrose density gradient. Three and two alkaline phosphatase froms from human and calf small intestines, respectively could be isolated by preparative isolectric focusing. The relative amounts of these components are not constant, but they have the same catalytic properties, suggesting that they may embody a common protein core with an identical active centre(s). Precipitating antisera for alkaline phosphatase from human and calf intestine have been prepard in rabbits by intramuscular, dermal, subcutaneous and intravenous administration of the pure major component of each enzyme species. Both antisera precipitate completely their homologous as well as their heterologous antigens (intestinal enzyme) and showed partial identity with placental alkaline phosphatase. There was no reaction with alkaline phosphatase from bone, liver heart, spleen, lung, stomach, pancreas, brain, bile-gall bladder and erythrocytes. Alkaline phosphatase preparation from human kidney contains a minor component of the intestinal type, beside many multiple forms which, on treatment with neuramindase, became identical in their electrophoretic and biochemical properties. At least eight multiple forms of the placental enzyme could be shown by isoelectric focusing in polyacrylamide gel. On treatment with neuraminidase these forms became less charged and only four forms remained. All forms were immunologically identical using either anti placental-enzyme or anti intestinal-AP serum. Monospecific antisera against human or calf intestinal alkaline phosphatase were obtained by absorption with purified placental enzyme. This monospecific anti intestinal-AP serum could be used for an immunological quantitative determination of the intestinal isoenzyme in sera or other liquids in the presence of other alkaline phosphatase isoenzymes.
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PMID:Alkaline phosphatase of human and calf small intestine. Purification and immunochemical characterization. 82 42

Alkaline phosphatase (EC 3.1.3.1) from human liver was purified to homogeneity. It is a glycoprotein of about 136000 molecular weight. Analysis of the subunit structure by sedimentation equilibrium in 6M urea and by dodecylsulfate polyacrylamide gel electrophoresis of the denatured enzyme indicated molecular weights of about 35000 and 32000, respectively. Thus, the human liver alkaline phosphatase seems to be a tetramer composed of identical or very similar subunits. The purified enzyme has a specific activity of 1360 mumol/(min x mg prot.), corresponding to a molecular activity of 3170s-1. The enzyme retains full activity in 1% sodium dodecylsulfate for several hours. The isoelectric point of the native enzyme is 4.2. After treatment with neuraminidase the isoelectric point increases to 6.5.
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PMID:Human alkaline phosphatases. I. Purification and some structural properties of the enzyme from human liver. 86 84

The serum alkaline phosphatase was fractionated by polyacrylamide gel electrophoresis in 317 patients with elevated serum alkaline phosphatase activity. In 253 patients the source of the elevation was the isoenzyme of presumed liver origin, band L. In 87 of these patients, there was either no obvious liver disease or the alkaline phosphatase elevation was inappropriately high. In 19 of the 87, liver disease was further excluded by liver biopsy or by laparotomy. Because of this, biochemical studies were done to verify the hepatic origin of band L. Band L and alkaline phosphatase extracted from human liver migrated together on polyacrylamide gel electrophoresis before and after digestion with Vibrio cholerae neuraminidase. They had identical pH optima, sedimentation coefficients, Michaelis constants, and rates of inactivation at 55.5 degrees C. They had different rates of inactivation in 3 M urea. Over-all, the data indicate that band L is of liver origin, and that elevation of the hepatic alkaline phosphatase isoenzyme may be a nonspecific finding in certain patients.
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PMID:Significance of elevated liver alkaline phosphatase in serum. 109 21

The effects of neuraminidase treatment on the electrophoretic pattern of alkaline phosphatase (AP) isozymes and AP activity were investigated in chicken plasma. AP comprised three isozymes. The zymogram of an individual chicken plasma had two bands, either the faster (F) or the slower (S) moving band by isozyme types and the B band irrespective of isozyme types. Mobility of the S band and AP activity in chicken plasma were not affected by neuraminidase treatment. The treatment has a reduced migration rate of the F band equal to that of the S band and the B band of both types closer to the origin. The genetic control of these bands is discussed.
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PMID:Further studies on the genetic control of chicken plasma alkaline phosphatase isozyme. 121 66

We adapted the electrophoretic method of bone alkaline phosphatase (ALP) determination using neuraminidase from Vibrio cholerae to separate bone and liver ALP on cellulose acetate membrane. Treatment of separator plus serum (1:8, neuraminidase 111 U/l in final) for 10 min at room temperature (25 +/- 1 degree C) and subsequent electrophoresis made it possible to quantify bone ALP activity simply and rapidly. The precision of the data was at the level of CV of 1.6% (within-day) and 4.7% (day-to-day), with recovery rates of 97-103%. The normal range of bone ALP activity depended on age and sex. Seventy-eight diabetes mellitus (DM) patients, excluding those with renal failure, were divided into two groups of those with and without osteopenia with matching of age (+/- 3 years) and sex. Bone ALP (P < 0.001) and total ALP (P < 0.05) activities and urine calcium/creatinine ratio (P < 0.05) were significantly higher in DM with osteopenia than in DM without osteopenia. Therefore, bone formation and absorption may be accelerated in DM with osteopenia in comparison with DM without osteopenia.
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PMID:Cellulose acetate electrophoretic determination of bone alkaline phosphatase activity in healthy subjects and diabetic patients with and without osteopenia. 142 53

Hyperphosphatasemia due to increased intestinal type serum alkaline phosphatase was noted in a 48-year-old male who had asymptomatic liver cirrhosis. The alkaline phosphatase activity in the serum was 828 U/l (our reference range in adults: 57-194 U/l), 94% of which was of the intestinal type as measured by an immunoprecipitation method. The intestinal component of alkaline phosphatase was separated into two major and some minor components using electrophoresis and isoelectrofocusing. One of the major components had similar mobility to that of a standard intestinal enzyme purified from adult intestine. The components were heat-labile and neuraminidase-resistant. Serial lectin affinity chromatography, however, indicated that sugar chain compositions of the alkaline phosphatase were different from those of the standard tissue intestinal enzyme. These results and further enzymological studies suggest that the patient's serum alkaline phosphatase basically consisted of several intestine-like isoforms.
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PMID:Intestinal type alkaline phosphatase hyperphosphatasemia associated with liver cirrhosis. 142 60


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