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)

Rats were injected with a single intravenous dose of aminonucleoside (AMN) and sacrificed 1-48 h later. The activity of several enzymes was assayed in the Golgi apparatus isolated from the liver. Galactosyltransferase activity showed little changes after the AMN, but both acid (EC 3.1.3.2) and alkaline phosphatase (EC 3.1.3.1) activities increased within the first hour and reached control levels only 5-24 h later. Thiamine pyrophosphatase and arylsulfatase A (EC 3.1.6.1) activities also increased and stayed at higher levels for the duration of the experiment. Arylsulfatase B (EC 3.1.6.1) activity decreased shortly after the AMN but later increased to above control levels. These findings support earlier results in which liver ultrastructural and biochemical changes were observed early before renal lesions and proteinuria.
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PMID:Early effects of aminonucleoside on enzymes in the Golgi apparatus of rat liver. 24 Apr 92

Preparations of intestinal epithelial cell basal lateral plasma membranes were analyzed with free flow electrophoresis and density perturbation with digitonin. The initial basal lateral membrane preparations were obtained by equilibrium density gradient centrifugation after two different schemes of homogenization and differential sedimentation (A.K. Mircheff, C.H. van Os, and E.M. Wright. 1978. Membr. Biochem. 1:177, and A.K. Mircheff, S.D. Hanna, M.W. Walling, and E.M. Wright. 1979. Prep. Biochem. 9:33. In these preparations, Na,K-ATPase, a marker for the basal lateral mambrane, was purified 16- to 18-fold over the initial homogenate. The preparations were also enriched in NADPH-cytochrome c reductase, alkaline phosphatase, acid phosphatase, and galactosyltransferase. Both free-flow electrophoresis, which separates on the basis of surface charge, and density perturbation with digitonin, which depends on a specific interaction of digitonin with cholesterol-rich membranes, resolved the preparation into three populations of particles. The major population, which represented basal lateral membranes purified 20- to 32-fold with respect to the initial homogenate, contained Na,K-ATPase, alkaline phosphatase, adenylate cyclase, and acid phosphatase. A second population was defined by its content of NADPH-cytochrome c reductase, and the third was defined by its content of galactosyltransferase. Guanylate cyclase appeared to be partitioned between the Na,K-ATPase-rich and NADPH-cytochrome c reductase-rich populations. Galactosyltransferase is also present in fractions which contain the Na,K-ATPase-rich membranes, but the present data cannot exclude the possibility of spillover by the adjacent, galactosyltransferase-rich population. This work emphasizes the importance of multiple, physical criteria for purity in the isolation of subcellular components.
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PMID:Highly purified basal lateral plasma membranes from rat duodenum. Physical criteria for purity. 51 18

Galactosyltransferase activity was assayed in sera from 58 patients with various types of cancer. On discontinuous polyacrylamide gel electrophoresis a slow-moving peak of galactosyltransferase activity (isoenzyme II) was found to be present in the serum of 43 of these patients in addition to the major isoenzyme I. Isoenzyme II was found in only 2 of 39 patients with various nonmalignant disorders and was not detected in the serum of 22 normal control subjects. There was no correlation between the presence of this electrophoretically distinct isoenzyme and total serum galactosyltransferase activity, alkaline phosphatase, levels of carcinoembryonic antigen, or blood type. However, patients with widespread metastases had significantly higher isoenzyme II levels than those with no metastases or with limited local spread. Further studies will be necessary to evaluate the clinical usefulness of this serum galactosyltransferase isoenzyme in the diagnosis and monitoring of patients with neoplastic disease.
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PMID:Cancer-associated isoenzyme of serum galactosyltransferase. 106 13

Rat liver microsomal fractions have been equilibrated in various types of linear density gradients. 15 fractions were collected and assayed for 27 constituents. As a result of this analysis microsomal constituents have been classified, in the order of increasing median density, into four groups labeled a, b, c, and d. Group a includes: monoamine oxidase, galactosyltransferase, 5'-nucleotidase, alkaline phosphodiesterase I, alkaline phosphatase, and cholesterol; group b: NADH cytochrome c reductase, NADPH cytochrome c reductase, aminopyrine demethylase, cytochrome b(5), and cytochrome P 450; group c: glucose 6-phosphatase, nucleoside diphosphatase, esterase, beta-glucuronidase, and glucuronyltransferase; group d: RNA, membrane-bound ribosomes, and some enzymes probably adsorbed on ribosomes: fumarase, aldolase, and glutamine synthetase. Analysis of the microsomal fraction by differential centrifugation in density gradient has further dissociated group a into constituents which sediment more slowly (monoamine oxidase and galactosyltransferase) than those of groups b and c, and 5'-nucleotidase, alkaline phosphodiesterase I, alkaline phosphatase, and the bulk of cholesterol which sediment more rapidly (group a2). The microsomal monoamine oxidase is attributed, at least partially, to detached fragments of external mitochondrial membrane. Galactosyltransferase belongs to the Golgi complex. Group a2 constituents are related to plasma membranes. Constituents of groups b and c and RNA belong to microsomal vesicles derived from the endoplasmic reticulum. These latter exhibit a noticeable biochemical heterogeneity and represent at the most 80% of microsomal protein, the rest being accounted for by particles bearing the constituents of groups a and some contaminating mitochondria, lysosomes, and peroxisomes. Attention is called to the operational meaning of microsomal subfractions and to their cytological complexity.
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PMID:Analytical study of microsomes and isolated subcellular membranes from rat liver. 3. Subfractionation of the microsomal fraction by isopycnic and differential centrifugation in density gradients. 415 Apr 90

We present a comparative study of several biological markers (galactosyltransferase, CA 125, isoenzymes of amylase and alkaline phosphatase) with a view to ovarian carcinoma follow-up. Serum samples were obtained from a population of 75 patients under clinical observation. After a minimum 18-months period, we assessed the prognostic value of the markers. No marker permits the detection of discrete, evolving carcinomas. CA 125 is the marker that gives the best results, particularly in terms of sensitivity. Galactosyltransferase has a lower sensitivity except in the case of endometrioid carcinomas. Simultaneous analysis with CA 125 and galactosyltransferase results in no decisive improvement, other than greater precision in unfavourable prognoses. Isoenzymes of amylase and alkaline phosphatase are of no interest in the follow-up of such carcinomas.
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PMID:Biological markers and ovarian carcinomas: galactosyltransferase, CA 125, isoenzymes of amylase and alkaline phosphatase. 752 19

Galactosyltransferase is required for the addition of galactose to lactosylceramide (galactose beta 1-4 glucose beta 1-1 ceramide), resulting in the synthesis of globotriaosylceramide (Gb3). We describe a quantitative more sensitive and specific method for the measurement of UDP-galactose:lactosylceramide galactosyltransferase activities in rabbit small intestine and HeLa cell which utilizes the specific binding of Shiga toxin to the product, Gb3. Intestinal microsomal or HeLa cell sonicate preparations were incubated in the presence of lactosylceramide and [14C]UDP-galactose. The lipid reaction products were extracted on C18 Bond-Elut columns, separated by high-performance thin-layer chromatography and exposed to Shiga toxin followed by polyclonal rabbit anti-Shiga toxin antibody and goat anti-rabbit IgG alkaline phosphatase conjugate. Gb3 was visualized with NBT and BCIP and quantitated by densitometry. These data were compared with a standard assay in which, following incubation and lipid extraction, radioactivity was measured by scintillation counting of the isolated lipids. There was a 22-fold increase in enzyme activity by the immunostaining method compared to the usual scintillation counting technique. This is attributable to the exclusion of radioactive lipids other than Gb3 in calculating enzyme activity and the correction for endogenous UDP-galactose. Thus, the immunostaining method provides increased accuracy, sensitivity, and specificity in the assay of galactosyltransferase activity.
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PMID:A quantitative immunostaining method for the measurement of UDP-galactose:lactosylceramide galactosyltransferase for the synthesis of globotriaosylceramide in rabbit small intestine and HeLa cells. 825 Feb 38

The lacrimal glands of males and females of various species differ with respect to several morphological, biochemical and functional characteristics. The purpose of this study was to determine the effect of sexual maturation on Na+,K(+)-ATPase, muscarinic cholinergic receptors and beta-adrenergic receptors, which are closely related to the secretion of electrolytes and fluid by the gland, and on other membrane-associated enzymes, specifically galactosyltransferase and alkaline and acid phosphatase. Soluble and total membrane fractions were obtained from lacrimal glands of prepubertal (1.0 kg), pubertal (2 kg), and mature (4 kg) of New Zealand white rabbits of both sexes. Prepubertal and pubertal rabbits exhibited no sex differences in the total amount of lacrimal gland protein or in any of the enzymes or receptors, with the exception of galactosyltransferase and alkaline phosphatase. Galactosyltransferase had higher total and specific activities in prepubertal and pubertal males, and alkaline phosphatase had higher specific activity in prepubertal males. As animals matured, total protein and activities of the enzymes increased, and several quantitative differences between males and females became apparent. Samples from mature females contained significantly less DNA and membrane and total protein. Specific activities of Na+,K(+)-ATPase, cholinergic receptors, galactosyltransferase, and acid and alkaline phosphatase were 40% to 80% greater (p < 0.05) in mature females. Total and specific activity for beta-adrenergic receptors, on the other hand, were higher in the male rabbits. These findings suggest that sex hormones play a role in regulating the levels of expression of a number of enzymes and receptors, including several which are clearly involved in lacrimal secretory functions.
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PMID:Sex-dependent parameters related to electrolyte, water and glycoprotein secretion in rabbit lacrimal glands. 826 91

In the intestinal brush border, the mechanoenzyme myosin-I links the microvillus core actin filaments with the plasma membrane. Previous immunolocalization shows that myosin-I is associated with vesicles in mature enterocytes (Drenckhahn, D., and R. Dermietzel. 1988. J. Cell Biol. 107:1037-1048) suggesting a potential role mediating vesicle motility. We now report that myosin-I is associated with Golgi-derived vesicles isolated from cells that are rapidly assembling brush borders in intestinal crypts. Crypt cells were isolated in hyperosmotic buffer, homogenized, and fractionated using differential- and equilibrium-density centrifugation. Fractions containing 50-100-nm vesicles, a similar size to those observed in situ, were identified by EM and were shown to contain myosin-I as demonstrated by immunoblotting and immunolabel negative staining. Galactosyltransferase, a marker enzyme for trans-Golgi membranes was present in these fractions, as was alkaline phosphatase, which is an apical membrane targeted enzyme. Galactosyltransferase was also present in vesicles immuno-purified with antibodies to myosin-I. Villin, a marker for potential contamination from fragmented microvilli, was absent. Myosin-I was found to reside on the vesicle "outer" or cytoplasmic surface for it was accessible to exogenous proteases and intact vesicles could be immunolabeled with myosin-I antibodies in solution. The bound myosin-I could be extracted from the vesicles using NaCl, KI and Na2CO3, suggesting that it is a vesicle peripheral membrane protein. These vesicles were shown to bundle actin filaments in an ATP-dependent manner. These results are consistent with a role for myosin-I as an apically targeted motor for vesicle translocation in epithelial cells.
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PMID:Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. 841 82

Galactosyltransferase activity was measured in the luminal plasma of the cauda epididymidis of mice, rats, rabbits, rams and boars, and in the rete testis fluid of rams and boars. The activities of nucleotide pyrophosphatase and alkaline phosphatase, which compete with galactosyltransferase for substrate, were also determined. In these species, galactosyltransferase activity in the luminal plasma of the cauda epididymidis was similar when the inhibitory effect of pyrophosphatase and phosphatase was minimized by assay conditions. However, under assay conditions that did not minimize the effect of these enzymes, the galactosyltransferase activities of these species were very different and were inversely correlated with the activities of pyrophosphatase and phosphatase. The ratio of galactosyltransferase activity to pyrophosphatase and phosphatase activity was much higher in the rete testis fluid than in the luminal plasma of the cauda epididymidis in both rams and boars. In rams, galactosyltransferase in the luminal plasma of the cauda epididymidis was more heat resistant than that in serum. These results suggest that there is a species difference in the availability of galactosyltransferase activity in the luminal plasma of the cauda epididymidis and that in some species, galactosyltransferase in the luminal fluid is unlikely to have any function. The results are also discussed with respect to the possible function of galactosyltransferase, pyrophosphatase and phosphatase in epididymal luminal plasma and rete testis fluid.
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PMID:Galactosyltransferase, pyrophosphatase and phosphatase activities in luminal plasma of the cauda epididymidis and in the rete testis fluid of some mammals. 1007 Mar 58