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Disease
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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)
6-Mercaptopurine (6MP) metabolism was quantitatively determined in L5178Y murine lymphoma. Cells grown in time-course incubates with [35S]-6MP were extracted with cold perchloric acid, and the buffered extracts were subjected to high-performance liquid cation-exchange chromatography prior to and after hydrolysis with
alkaline phosphatase
. Free
sulfate
, 6-thiouric acid, 6-thioxanthosine, 6-thioguanosine, 6-thioinosine, free 6MP, and 6-methylthioinosine were separated from each other; identified in the radiochromatograms by elution volume, UV spectroscopic data, and enzymatic peak-shifting analyses with purine nucleoside phosphorylase; and quantitatively determined by means of 35S radioactivity. Gross intracellular 35S concentrations remained constant at 5 x 10(-5) M after 1 hr of incubation. 6MP metabolism in L5178Y cells was distinguished into an early phase (to 1 hr of incubation) in which 6MP was predominantly catabolized to 6-thiouric acid and free
sulfate
, into an intermediate phase (to 8 hr) in which substantial amounts of free 6MP and of ribonucleotides of 6-thioxanthosine and 6-thioguanosine were present while the concentrations of nonnucleotide oxidation products sharply decreased, and into a late phase (to 24 hr) in which the ribonucleotides of 6MP, of 6-thioguanosine and, in particular, of 6-methylthioinosine were the most abundant metabolites.
...
PMID:Quantitation of intracellular metabolites of [35S]-6-mercaptopurine in L5178Y cells grown in time-course incubates. 47 98
The isolation of plasma membranes is often accompanied with a loss of sensitivity to stimulatory agents (e.g. mitogens). Changes in the structure of the cell membranes after cell breakage have also been reported. Concerning this problem, "mild" cell disruption conditions were tested by using osmotic shock. Different membrane fractions were isolated, resulting in an enrichment of plasma membranes in one fraction. All fractions were characterized by plasma membrane marker enzymes (
alkaline phosphatase
, gamma-glutamyltransferases), the amount of cholesterol, the molar ratio of cholesterol and phospholipid, by dodecyl
sulfate
-gelectrophoresis and by electronmicroscopy. Total balance sheets of the fraction were made for each of the different biochemical parameters. The enriched plasma membranes resulting by using the described method had also lost the sensitivity to the stimulatory effect caused by mitogens such as Concanavalin A.
...
PMID:Preparation and fractionation of membrane vesicles of thymocytes after osmotic cell disruption. 51 Nov 18
Alkaline phosphatase [orthophosphoric monoester phosphohydrolase,
EC 3.1.3.1
] was purified from the mucosa of rat small intestine by butanol extraction, ethanol fractionation, gel filtration, with controlled-pore glass-10 and DEAE-cellulose column chromatography. On the gel filtration, the enzyme activity was separated into three peaks; A in the void volume, B and C at lower molecular weight positions. Enzyme A was purified to homogeneity. The activity of enzymes A, B, and C was detected even on sodium dodecyl
sulfate
-polyacrylamide gel electrophoresis at the position of the protein of enzyme A, which had a molecular weight of 110,000 daltons. Enzymatic properties such as pH optimum, Km value for the substrate, heat inactivation and inhibition by amino acids were the same in all three enzymes. Based on these findings, together with the elution positions on gel filtration, enzyme A was regarded as an aggregate, and enzymes B and C as dimer and monomer molecules, respectively.
...
PMID:Purification and properties of alkaline phosphatase from the mucosa of rat small intestine. 52 34
Fecal proteins from germfree and conventional rats were isolated. The proteins from the two kinds of feces differed in molecular weight, judging from Sephadex gel filtration and sodium dodecyl
sulfate
-polyacrylamide gel electrophoresis. The conventional feces contained a greater amount of high-molecular-weight and a lesser amount of low-molecular-weight proteins than did the germfree feces. The fecal proteins of both kinds contained carbohydrates. Both feces contained considerable enzyme activity. The germfree feces contained extremely high activity in
alkaline phosphatase
and leucine aminopeptidase. Both feces showed the same level of trehalase activity. The conventional feces contained higher levels of activity of protease and acid phosphatase than did the germfree feces. Lactase activity was observed only in the conventional feces. The fecal
alkaline phosphatase
resembled the intestinal enzyme in response to L-phenylalanine inhibition and urea denaturation. From these results it was inferred that the germfree feces contained some of the intestinal proteins and that the conventional feces contained bacterial proteins in addition to intestinal proteins.
...
PMID:Isolation and properties of fecal proteins and fecal alkaline phosphatase from germfree and conventional rats. 63 36
The relationship between the structure and function of
alkaline phosphatase
(orthoposphoric monoester phosphohydrolase (alkaline optimum),
EC 3.1.3.1
) isoenzymes is under investigation in a number of laboratories. The present study deals with the effects of glycosidase digestion on the
alkaline phosphatase
isoenzymes. Changes in physicochemcial properties, activity, affinity for various lectins and blood group antisera, carbohydrate composition and biological half-life were investigated. The desialylated hepatic enzyme was shown to be more heat labile and more sensitive to protease digestion in the presence of 0.5% sodium dodecyl
sulfate
than native hepatic enzyme. Helix contents of the native and desialated hepatic enzyme were calculated to be 39.0 and 30.8%, respectively, and apparent molecular weights 175,000 and 167,000, respectively. Intestinal enzyme preparations treated with alpha-mannosidase, exo-N-acetyl-Dglucosaminidase and endo-N-acetyl-D-glucosaminidase-D displayed a decrease in enzyme activity. Among these, the alpha-mannosidase-treated enzyme activity was the most clearly reduction. The maximum activity of the alpha-mannosidase-treated intestinal enzyme was observed to change from 40 mM Mg2+ to 5--10 mM Mg2+.
...
PMID:The function of carbohydrate moiety and alteration of carbohydrate composition in human alkaline phosphatase isoenzymes. 65 34
Studies are presented of the effect of procaine group anesthetics on rat brain synaptosome stability to dodecyl
sulfate
and on catalytic properties of the membrane bound
alkaline phosphatase
. The dose curves of detergent stability are characterized by two maxima, one at 3.10(-4) M for tetracaine, 2.10(-6) M for lidocaine and 5.10(-5) M for procaine; the other being at 10(-3) M for all anesthetics. The curves of Vmax and KM versus procaine concentration to exhibit the minimum at 5.10(-7) M and maximum at 3,2.10(-6) M. Procaine at 5.10(-7) M increases enthalpy and enthropy of membraneous
alkaline phosphatase
. It is suggested that interactions between anesthetics and centers of high affinity lead to synaptosome structural rearrangements, which affect the properties of membraneous enzymes.
...
PMID:[Effect of physiologic concentrations of local anesthetics of the procaine series on the structural and functional state of cerebral synaptosome membranes]. 69 53
The metabolism of ground substance in connective tissue of an 18-year-old boy with oculo-cerebro-renal syndrome was studied. He had characteristic clinical and laboratory findings described by Lowe et al. such as growth retardation, mental deficiency, glaucoma, cataracta, decreased muscle tone, metabolic acidosis, aminoaciduria and osteomalacia. The urinary excretion of acid glycosaminoglycans and of total hydroxyproline were 27 mg/day (as glucuronic acid) and 280 mg/day respectively on admission. Both values decreased to the upper limits of normal level transiently during treatment with alkali and vitamin D2. At that time, an improvement in bone abnormalities, a decrease of serum
alkaline phosphatase
, and an elevation of serum inorganic phosphate were observed. The therapy prevented him from progressive osteomalacia and cured him of it, but mucopolysacchariduria and hydroxyprolinuria did not disappear. Analytical electrophoresis on cellulose acetate sheets showed that urinary acid glycosaminoglycans were composed of undersulfated chondroitin 4-/6-
sulfate
and heparan
sulfate
with a ratio of 6:4, on admission. After oral administration of alkali, the excretion of heparan
sulfate
decreased and undersulfated chondroitin 4-/6-
sulfate
was determined as a main component of urinary acid glycosaminoglycans. The clinical and laboratory data in this case suggested that the increased excretion of acid glycosaminoglycans and total hydroxyproline was caused by abnormal metabolism in connective tissues, especially by the bone abnormalities, in this syndrome.
...
PMID:Urinary excretion of acid glycosaminoglycans and hydroxyproline in a patient with oculo-cerebro-renal syndrome. 73 46
Brush border membrane vesicles were isolated from rat kidney cortex by differential centrifugation in the presence of 10 mM calcium. Their properties were compared to brush border vesicles isolated by free-flow electrophoresis. By the calcium precipitation method membrane vesicles were obtained in a shorter time with a similar enrichment of brush border marker enzymes (11- to 12-fold for
alkaline phosphatase
and maltase), with a similarly reduced activity of the marker enzyme for basal-lateral plasma membranes and an almost identical protein composition as revealed by polyacrylamide gel electrophoresis in sodium dodecyl
sulfate
. The transport properties of the two membrane preparations for D-glucose, L-phenylalanine, and phosphate are essentially the same; there is some indication for a lower sodium permeability of the vesicles prepared by the calcium precipitation method. The latter vesicles were also shown to exhibit sodium gradient stimulated uptake of L-glutamate.
...
PMID:Properties of brush border vesicles isolated from rat kidney cortex by calcium precipitation. 75 88
A randomized, double blind crossover study of the effects of zinc
sulfate
and placebo was carried out in 106 patients with taste and smell dysfunction secondary to a variety of etiological factors. In the patient group prior to treatment, mean serum zinc concentration and leukocyte
alkaline phosphatase
activity were significantly lower than normal. Results indicate that zinc
sulfate
was effectively equivalent to placebo in the treatment of these disorders. Although these results demonstrate abnormalities of zinc metabolism in some patients with taste and smell dysfunction they fail to provide evidence for a single, therapeutic approach to the many disorders which are associated with abnormalities of taste and smell. However, the methods and procedures developed in this study demonstrate that taste and smell dysfunction can be studied in a quantitative, systematic manner.
...
PMID:A double blind study of the effects of zinc sulfate on taste and smell dysfunction. 79 59
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.
...
PMID:Alkaline phosphatase of human and calf small intestine. Purification and immunochemical characterization. 82 42
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