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)

Bile duct ligation in the rat leads to a rapid increase in hepatic and serum alkaline phosphatase activity. Within 12 hr after bile duct ligation, hepatic alkaline phosphatase has increased 7-fold and serum alkaline phosphatase activity 2(1/2)-fold. The elevation in the serum activity is completely due to an increase in an isozyme that appears to originate in the liver. This serum isozyme and liver phosphatase, both partially purified by DEAE-cellulose column chromatography, have identical Michaelis constants, pH optima, and rates of heat denaturation. These isozymes migrate identically when subjected to electrophoresis on polyacrylamide gel, and their migration rates are equally slowed after neuraminidase digestion. The data suggest that the rise in hepatic alkaline phosphatase activity is dependent on de novo protein synthesis. Cycloheximide, in a dose that inhibited incorporation of leucine-(14)C into protein by 68%, inhibited the rise in liver phosphatase by 98% and that in serum by 80%. The rise in liver phosphatase activity could not be accounted for by simple retention of alkaline phosphatase that would normally appear in bile. The rise in liver activity after bile duct ligation was 240 times greater than the amount of phosphatase that normally appears in bile over a similar period of time. Cycloheximide had no effect on the bile duct ligation-induced changes in the serum and liver glutamic pyruvic transaminase.
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PMID:Induction of rat liver alkaline phosphatase: the mechanism of the serum elevation in bile duct obstruction. 541 76

1. Two alkaline phosphatase fractions from sheep brain obtained by DEAE-cellulose column chromatography were shown to be associated with different concentrations of NANA (N-acetylneuraminic acid). Enzyme II contains nearly three times as much NANA as does enzyme I. 2. Partial removal of NANA by neuraminidase digestion from these alkaline phosphatase fractions has different effects on their chromatographic properties. Though the enzymic release of NANA has no effect on the elution pattern of enzyme I from a DEAE-cellulose column, such a treatment shifts the elution pattern of enzyme II towards that of enzyme I. 3. However, this change in the elution pattern of enzyme II as a result of the removal of NANA does not produce any change in the kinetics of this fraction, and the differences between enzyme I and enzyme II with respect to their substrate affinities and K(i) for phosphate inhibition are maintained even after the removal of NANA. 4. Results indicate that NANA is not the only factor responsible for the heterogeneity of alkaline phosphatase in sheep brain and enzyme I is not the result of the removal of NANA from enzyme II.
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PMID:Role of neuraminic acid in the heterogeneity of alkaline phosphatase in sheep brain. 564 74

1. Four fractions of kidney alkaline phosphatase were prepared by chromatography on DEAE-Sephadex. An investigation of their properties suggests that the fractions represent modifications of a single kidney enzyme. 2. Urinary alkaline phosphatase resembles kidney enzyme in most of its properties, but differs in K(m) and in the degree by which it is activated by Mg(2+) ions. 3. Estimates of the molecular weights of kidney and urinary alkaline phosphatase gave values of 150000-170000 for kidney phosphatase and 75000 for the urinary enzyme. 4. It is suggested that urinary alkaline phosphatase is a sub-unit of kidney phosphatase, but it has not been possible to simulate the formation of urinary enzyme by treating kidney enzyme with urea or H(+) ions.
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PMID:Human kidney and urinary alkaline phosphatases. 566 Jun 28

1. The purification of a nuclease from rat-liver mitochondria is described. The mitochondria are rendered soluble by treatment with Triton X-100 and, after fractionation with ammonium sulphate and acetone, the active fraction is further purified by chromatography on DEAE-cellulose and Sephadex G-75 to give a purification of over 700-fold. 2. The purified enzyme was only very slightly contaminated with deoxyribonuclease II, phosphodiesterase and phosphomonoesterase. The individual activities of these enzymes did not exceed 0.1% of the activity of the liver nuclease. 3. The purified enzyme attacked RNA more rapidly than denatured DNA and hydrolysed native DNA more slowly than denatured DNA. 4. There is some evidence to suggest that the nucleolytic activity of the purified preparation towards native DNA, denatured DNA and RNA is associated with a single protein. 5. The enzyme is relatively labile but is stabilized in the presence of 20% (w/v) glycerol or 10mm-2-mercaptoethanol.
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PMID:The purification from rat liver of a nuclease hydrolysing ribonucleic acid and deoxyribonucleic acid. 591 28

The brain-specific arylsulfatase Bm (aryl-sulfate sulfohydrolase, EC 3.1.6.1) was demonstrable in human and monkey brain. Arylsulfatases A, B and Bm were separated employing DEAE-cellulose chromatography. There was a distinct difference in the proportion of the sulfatases in infant and adult human brain. Arylsulfatase Bm after concanavalin A-Sepharose chromatography showed the property of binding to Sephadex G-200 totally. Several dissociating agents failed to elute the enzyme from the bound form. Under similar conditions arylsulfatase A did not show any binding to Sephadex. On treatment with Escherichia coli alkaline phosphatase adult human brain arylsulfatase Bm but not arylsulfatase A was converted into a less acidic, presumably dephosphorylated form that did not bind to DEAE-cellulose. Monkey brain arylsulfatase Bm showed a similar susceptibility to E. coli phosphatase treatment. Inorganic phosphate and serine phosphate but not mannose 6-phosphate could inhibit this dephosphorylation. There were differences in the susceptibilities to alkaline phosphatase treatment of the arylsulfatase Bm from infant and adult human brain. Endogenous phosphatase also seemed to have a role on the phosphorylated state of arylsulfatase Bm.
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PMID:Soluble arylsulfatases of human brain and some characteristics of the brain-specific arylsulfatase Bm. 610 86

Tyrosine hydroxylase (TH) in freshly prepared 45,000 g supernatant from rat striatum was fractionated by DEAE-cellulose chromatography. The elution was made with 2 vols. of buffer (50 mM Tris, pH 7.4; 2 mM dithiothreitol) followed by 4 vols. of a linear NaCl gradient (0 0.3 M) in the same buffer. TH activity was eluted in two distinct peaks: one at about 0.1 M salt (I), and the other at 0.2 M salt (II). The relationship between the two enzymes peaks was examined as follows. (1) Incubation of the supernatant in the presence of cAMP-dependent protein kinase, 1 mM ATP, 10 mM Mg2+, and 0.1 mM cAMP resulted in the elimination of peak I, with a concomitant increase of peak II. This shift of TH peaks was prevented when the protein kinase was blocked by the addition of its inhibitory modulator. (2) Incubation of the supernatant with alkaline phosphatase, an enzyme known to dephosphorylate a variety of phosphoproteins, resulted in the elimination of peak II, with a concomitant increase of peak I. (3) Only freshly prepared supernatants showed two distinct TH peaks from DEAE-cellulose. From supernatants held at 0 degrees C for 24 h. peak II was markedly reduced and peak I concomitantly increased. Since peak II appears to be readily convertible to peak I, no further fractionation was attempted. From the data obtained here, we believe that peaks I and II are respectively the nonphosphorylated and phosphorylated forms of TH. Furthermore, the endogenous distribution of the two TH forms in striatum was altered by the administration of haloperidol (2 mg/kg. i.p.), a neuroleptic drug known to activate the enzyme via a cAMP-dependent mechanism. At 90 min after the treatment, there was a marked increase of peak II, with a concomitant decrease of peak I. Thus, this procedure provides a simple means for estimating the degree of phosphorylation of TH in vivo in catecholaminergic neurons under various physiological and pharmacological conditions.
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PMID:Two forms of striatal tyrosine hydroxylase from DEAE-cellulose chromatography. 613 70

ATP pyrophosphohydrolase was partially purified from fetal bovine epiphyseal cartilage. The purification was about 10- and 100-fold over the enzyme activities of matrix vesicle fraction and cell homogenate, respectively. The pyrophosphohydrolase and alkaline phosphatase were separated by a sequential application of Sepharose CL-6B and DEAE-cellulose column chromatographies. The purified enzyme migrated as a single band corresponding to the molecular weight of 230,000 in sodium dodecyl sulfate-polyacrylamide disc gel by electrophoresis. The enzyme absolutely required Zn2+ for its activity and appeared to bind Zn2+ strongly with an apparent affinity of p[Zn2+]0.5 = 13.4. The apparent Km for ATP was 0.18 mM. The enzyme was also reactive toward various nucleoside triphosphates including GTP, CTP, and UTP. In contrast, various phosphodiesters including RNA, UDP-glucose, NAD, and bis-p-nitrophenylphosphate were 5% or less as reactive as the nucleoside triphosphates. The pyrophosphohydrolase was inactive toward adenosine 3':5'-monophosphate or various phosphonates. UDP-glucose (1 mM), NAD (1 mM), or RNA (1 mg/ml) failed to inhibit the ATP pyrophosphohydrolase activity. These observations suggest that the ATP pyrophosphohydrolase of the cartilage is probably not a phosphodiesterase I. The matrix vesicle fraction, which probably also included some plasma membrane vesiculated during collagenase digestion, contained the highest specific activity of the enzyme as compared to other subcellular fractions of either epiphyseal or articular cartilage.
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PMID:Purification and partial characterization of ATP pyrophosphohydrolase from fetal bovine epiphyseal cartilage. 621 90

For setting up an Enzyme-Linked Immunosorbent Assay (ELISA) to detect antibodies to herpes simplex virus type 1 (HSV-1), the virus was propagated in Vero cells and partially purified by sonification and ultracentrifugation on 30% sucrose solution. DEAE ion-exchange column chromatography was used for purification of goat anti-human IgG serum. The anti-human IgG immune serum and alkaline phosphatase were conjugated by glutaraldehyde method. ELISA test was performed by reacting HSV-1 antigen coated in polystyrene tubes with serum specimens and enzyme-IgG conjugates. The color produced by enzyme-substrate reaction was measured on a spectrophotometer. The results obtained by the ELISA had a good agreement with those obtained by a standard neutralization procedure on 119 serum specimens tested for antibody to HSV-1.
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PMID:Detection of serum antibody to herpes simplex virus type I by enzyme-linked immunosorbent assay (ELISA). 626 77

Guinea pig epidermal DNAase I was purified from an epidermal extract by a procedure including DEAE-cellulose chromatography, Sephadex G-100 gel filtration and Con A-Sepharose affinity chromatography. The purified enzyme contained no detectable activities of acid DNAase, alkaline RNAase, phosphodiesterase or acid or alkaline phosphatase, but was contaminated with acid RNAase activity. The molecular weight of the enzyme was estimated to be 33 000 by sucrose density gradient centrifugation and Sephadex G-100 gel filtration. Its isoelectric point is 5.2 +/- 0.1. The enzyme requires divalent cations and exhibits two pH optima that are dependent on divalent cations: in the presence of Mn2+, the optimum pH is about 7.5 in 50 mM Tris-HCl buffer and in the presence of Mn2+, the pH is 6.4 in 50 mM cacodylate-HCl buffer. The enzyme hydrolyzes native DNA about 6-times faster than denatured DNA, producing 5'-phosphoryl and 3'-hydroxyl terminated oligonucleotides with an average chain length of about eight nucleotides, and converts double-stranded and circular DNA to relaxed and linear forms. The enzyme is inhibited by G-actin and antiserum against bovine pancreatic DNAase A. Thus this enzyme is classified as DNAase I.
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PMID:Purification and properties of a neutral endodeoxyribonuclease from guinea pig epidermis. 627 8

Extracts of human intestinal mucosa were examined for their ability to hydrolyze various phosphodiester, phosphomonoester and phenylphosphonate ester linkages. Enzymes carrying out these reactions were partially purified by butanol extraction, ammonium sulfate precipitation and DEAE-cellulose chromatography, and examined for polymorphism on polyacrylamide gels. Two species of alkaline phosphatase and at least five species of PDE I were identified. Antibodies to purified bovine intestinal phosphatase and phosphodiesterase were found specific for the respective human enzymes.
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PMID:Tissue specificity of human phosphodiesterase. II. Intestinal mucosa. 630 34


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