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)

Investigations were carried out on the alkaline phosphatase in the sera of cattle, horses, pigs, sheep, goats, and chickens, the pH value of the buffer used being 9.0-9.8-10.0-10.2-10.6 and 11.0, and the method applied--that of Richterich. The pH value at which the serum alkaline phosphatase in the various farm animals and birds was most active was found to vary to a large extent. Optimal values for the enzyme's activity usually range as follows: cattle, 10.2; pigs and goats, 10.0; sheep,--10.2; horses,--9.8; chickens,--10.6.
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PMID:[Comparative study of the optimum pH value of serum alkaline phosphatase in various species of farm animals]. 0 2

The diagnostic specificity of a new method to detect obstructive jaundice by determination of lipoprotein X (LP-X) was tested in 144 patients with different kinds of hepatic diseases and compared with the usual chemical "obstructive jaundice specific" tests, such as bilirubin, SGOT, SGPT, alkaline phosphatase, LAP and gamma-GT. The LP-X test was performed by using all-in test kit LP-X Rapidophor" low-voltage electrophoresis of Immuno AG/Wien. The results were correlated with the histological classification of the liver biopsy specimen. In 82% of the histologically verified cases of obstructive jaundice the result of the LP-X test was positive, whilst in 98.5% of the histologically negative cases the result of the LP-X test was negative. Hence, this LP-X method proved superior to chemical methods in providing a clear-cut positive or negative answer to the presence of cholestasis. Furthermore, the LP-X test was suitable for long-term follow-up investigation of patients with obstructive jaundice.
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PMID:[The diagnosis of cholestasis: lipoprotein X (LP-X) (author's transl)]. 0 12

The alkaline phosphatase reaction is normally absent in human bile canaliculi, but was found in 79 patients. In search for a common causal factor, these patients were further examined. Thirty-seven were autopsied. The conditions most ocmmonly associated with the phenomenon were malignant tumours with or without involvement of the liver, collagen diseases, long-standing partial obstruction of the common bile duct, and genetic variants of alpha-1-antitrypsin. No clinical or laboratory facts were common to all the patients.
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PMID:Bile canalicular alkaline phosphatase and disease. 0 42

There was a high activity of alkaline phosphatase in the blood plasma of piglets during the first few days of live; enzyme obtained at this time had high heat stability and was readily inhibited by L-phenylalanine (5 mM). The enzyme in blood was inhibited to a greater extent than alkaline phosphatase from intestinal mucosa. With increasing age there was a fall in heat stability and in the ease with that the enzyme could be inhibited by phenylalanine. The proportion of alkaline phosphatase derived from bone and present in blood plasma increased with increasing age. Two isoenzymes were detected in liver, kidney, lung, intestinal mucosa and endometrial mucosa by electrophoresis in polyacrylamide gel. Heat lability and inhibition by phenylalanine were good criteria for differentiating different types of alkaline phosphatase in pigs. In the case of alkaline phosphatase in blood plasma, disodium phenylphosphate was split more readily than p-nitrophenyl phosphate and very much more readily than phenolphthalein diphosphate and beta-glycerophosphate.
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PMID:[Activity and properties of alkaline phosphatase in the plasma and various organs (kidney, liver, small intestine mucosa, bone) of the swine]. 0 84

Human placental microsomal 5'-nucleotidase (EC 3.1.3.5) was prepared free of alkaline phosphatase by isoelectric focusing. A total of seven electrophoretic variants were isolated during the preparation of six placentas. Only three to six variants were found in a single placenta. The isoelectric pH's were 6.70, 6.44, 6.23, 6.02, 5.76, 5.63 and 5.44. These were found to be composed of variable quantities of a large, medium and low molecular weight form. The apparent molecular weights of the medium and light form of the enzyme were 86 500 and 43 500, respectively, as estimated from Stokes radius and sedimentation velocity determinations. The electrophoretic variants were not distinguishable with respect to specific activity and Michaelis constants for AMP, GMP or CMP or inhibition by ATP, CTP or adenosine. These electrophoretic variants appeared to be pseudoisozymes based upon different states of aggregation of a common primary sequence. There was a wide range of substrate specificity among nucleoside 5'-monophosphates which included 2-deoxyribose compounds. With AMP as 100, substrate activity was: CMP, 122; NMN, 74; GMP, 68: IMP, 63; XMP, 28 and UDP-glucose, 68. The Michaelis constants for AMP, GMP and CMP ranged from 12-18 muM, from 33-67 muM and from 170-250 muM, respectively. Although 5'-nucleotidase was active in the absence of divalent cation, 5 mM MgCl2 stimulated the enzyme activity to 234% of control and shifted the pH optimum of 9.8 to a plateau from pH 7.4-9.8.
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PMID:Purine catabolism in man: characterization of placental microsomal 5'-nucleotidase. 0 35

I studied the kinetics and sensitivity toward inhibition by levamisole and R 8231 of the most important human alkaline phosphatase isoenzymes. N-Ethylaminoethanol proved superior to the now widely used diethanolamine buffer, especially for the enzymes from the intestine and placenta, behaving as an uncompetitive activator. The optimum pH largely depends on the substrate concentration. The addition of Mg2+ has no effect on the activities. The meaning of Km-values for alkaline phosphatases is questioned. Isoenzymes from human liver, bone, kidney, and spleen are strongly inhibited by levamisole or R 8231 at concentrations that barely affect the enzymes from intestine or placenta. The inhibition is stereospecific, uncompetitive, and not changed by Mg2+. Inhibition is counteracted by increasing concentrations of N-ethylaminoethanol. The mechanism of inhibition is suggested to be formation of a complex with the phosphoenzyme.
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PMID:Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans. 0 69

Soluble alkaline phosphatase from Thiobacillus thioparus cells was purified about 230-fold. The enzyme had a mol. wt. of 50 000 daltons, optimum pH at 10.5, and was heat-resistant in the presence of diethanolamine. Polyacrylamide-gel electrophoresis demonstrated contamination of the preparation with inactive proteins and the presence of two active bands. The enzyme activity was distinctly stimulated by increasing concentrations of Tris or diethanolamine. In the presence of glycine, 1 mM-Zn2+ enhanced the enzyme activity; in Tris or diethanolamine buffers the activity was stimulated by 1 mM-Mg2+ whereas Zn2+ had a strong inhibitory effect. Glycine at concentrations exceeding 25 mM also inhibited the enzyme. Specificity of the enzyme is fairly broad.
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PMID:Alkaline phosphatase of Thiobacillus thioparus. Partial purification and properties of the enzyme. 0 90

A method using p-benzoquinone for coupling antigens and antibodies to enzymes and erythrocytes is described. The method involves the treatment of proteins (or polysaccharides) at pH 6 or 7 with an excess of p-benzoquinone. After removal of the unreacted reagent by gel filtration, the "activated" proteins were coupled at pH 8-9 with enzymes or erythrocytes. Biological activities of the proteins were not substantially modified by this treatment since 80-100% of the antigen binding capacity was found to be preserved in p-benzoquinone treated antibodies or Fab fragments. Anti-Ig antibodies (or Fab) were coupled by this procedure to peroxidase, alkaline phosphatase, lactoperoxidase, glucose oxidase and beta-galactosidase, and the conjugates obtained were found to be highly effective in detecting intracellular Ig by immunohistochemical techniques. Erythrocytes coated with sheep anti-mouse Ig antibody or Fab were used to titrate by passive hemagglutination serum Ig. The same erythrocytes were employed to detect by plaque assay mouse Ig secreting cells. Erythrocytes coated with peroxidase, alkaline phosphatase, bovine serum albumin, ribonuclease, Salmonella polysaccharide (B 27 +) and pneumoccocal polysaccharide SIII were employed to titrate serum antibody by passive hemagglutination and hemolysis and to detect mouse antibody secreting cells by plaque assay. All the antigens and antibodies coated erythrocytes prepared gave highly satisfactory and reproducible results.
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PMID:A new method using p-benzoquinone for coupling antigens and antibodies to marker substances. 0 79

The kinetic study of the C2+ ATPase activity of lymphocyte plasma memebranes allowed some properties of this enzyme to be evidenced. The Ca2+-activated hydrolysis of ATP is independent of a non-specific alkaline phosphatase. The substrate of the ATPase activity is the chelate Ca2+- ATP. Mg2+ may substitute for Ca2+ both as chelating ion and as activating ion. Several results suggest that we have only one ATPase, activated either by Ca2+-, or by Mg2+ with less efficiency; both chelates hve the same Km; pH values for maximum activity and transition temperatures are identical; the effects of free ions are also the same, activation at low concentration and inhibition at high concentration.
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PMID:[Kinetics of Ca 2+ or Mg 2+ activated ATPase from lymphocyte plasma membranes]. 0 56

It is known that the composition and character of human saliva alters during the menstrual cycle, presumably in response to changes in the level of ovarian hormones. A clinical study was undertaken to determine cyclic variations in salivary enzymes. Saliva from 4 healthy women aged 20-31 with a history of normal menstrual cycles were studied. The laboratory procedures performed on the saliva samples--from 6 menstrual cycles--are described and the results are graphed. Exfoliated cells from the oral mucosa were the main source of these enzymes. In all the cycles, alkaline phosphatase activity peaked sharply at mid-cycle, close to the expected time of ovulation; in 5 of the cycles, the peak occurred before the postovulation rise in body temperature. The levels of arylsulfatase and beta-glucuronidase, studied in 2 consecutive cycles of 1 woman, peaked in the periovulatory phase. All 3 enzymes were elevated during the luteal phase of the cycle as well. Increased cellular content of the saliva is attributed to the elevated circulating blood estrogen levels in the immediate preovulatory and midluteal phases of the cycles. There is great variability among subjects, however. Before a simple test for ovulation by home measurement of salivary enzymes can be developed, an ajustment of the test sensitivity would be necessary for adaptation to the individual woman.
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PMID:Alkaline phosphatase, arylsulfatase and beta-glucuronidase in saliva of cyclic women. 0 94


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