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)

The API STAPH-IDENT system was compared with conventional methods for the identification of 14 Staphylococcus species. Conventional methods included the Kloos and Schleifer simplified scheme and DNA-DNA hybridization. The API STAPH-IDENT strip utilizes a battery of 10 miniaturized biochemical tests, including alkaline phosphatase, urease, beta-glucosidase, beta-glucuronidase, and beta-galactosidase activity, aerobic acid formation from D-(+)-mannose, D-mannitol, D-(+)-trehalose, and salicin, and utilization of arginine. Reactions of cultures were determined after 5 h of incubation at 35 degrees C. Results indicated a high degree of congruence (greater than 90%) between the expedient API system and conventional methods for most species. The addition of a test for novobiocin susceptibility to the API system increased the accuracy of identification of S. saprophyticus, S. cohnii, and S. hominis, significantly. Several strains of S. hominis, S. haemolyticus, and S. warneri which were difficult to separate with the Kloos and Schleifer simplified scheme were accurately resolved by the API system.
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PMID:Identification of Staphylococcus species with the API STAPH-IDENT system. 675 90

Polypeptides of 61,500 and 64,500 apparent molecular weights were the precursor and fully processed forms of placental alkaline phosphatase monomer synthesized by choriocarcinoma cells in vivo. [3H] Mannose was incorporated into both polypeptides whereas [3H] glucosamine was incorporated mainly into the 64,500-dalton polypeptide, suggesting processing by the addition of glucosamine moieties. In the absence of microsomal membranes, choriocarcinoma mRNA directed the cell-free synthesis of the preprotein form of alkaline phosphatase monomer of apparent Mr = 60,000. The unglycosylated monomer had an apparent Mr = 58,000. In the presence of microsomal membranes, the 60,000-dalton polypeptide was processed to a polypeptide of apparent Mr = 61,500, comigrating with the precursor form of alkaline phosphatase monomer.
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PMID:Biosynthesis and processing of placental alkaline phosphatase. 683 75

Biochemical response to the toxic lung damage induced by inhalation of methylene chloride was studied. Significant increases in protein, hexose, sialic acid, lactate dehydrogenase, acid and alkaline phosphatase content were observed in the cell-free lavage effluents from lungs of exposed rats compared to the control animals. This was interpreted as increased cell damage accompanied by enhanced pulmonary secretions, perhaps of glycoproteins and mucins, as a result of inhalation toxicity.
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PMID:Biochemical studies on pulmonary response to inhalation of methylene chloride. 689 68

Carboxypeptidase Y, a vacuolar enzyme from Saccharomyces cerevisiae, was digested with endo-beta-N-acetyl-D-glucosaminidase H to release the four oligosaccharide chains that are linked to asparagine in the glycoprotein. The oligosaccharides were fractionated into a neutral and acidic component, and the latter proved to phosphorylated. From its gel filtration pattern, the neutral fraction was shown to be a mixture of at least four homologs, the smallest of which had a proton NMR spectrum almost identical to that given by an IgM oligosaccharide with eight mannoses and one N-acetylglucosamine [Cohen, R. E. & Ballou, C. E. (1980) Biochemistry 19, 4345--4358]. The yeast oligosaccharide has one additional mannose unit in an alpha 1 leads to 3 or alpha 1 leads to 6 linkage, whereas the larger homologs appear to have two, three, and four more mannose units. One phosphorylated oligosaccharides with a mannose/phosphate ratio of 12.5 was reduced with NaB3H4 and then subjected to mild acid hydrolysis. This released mannose and mannobiose that were glycosidically linked to the phosphate group, whereas complete acid hydrolysis yielded D-mannose 6-phosphate. The recovered oligosaccharide phosphomonoester, which contained 11 or 12 mannose units, was digested exhaustively with alpha-mannosidase, and the product of this reaction was treated with alkaline phosphatase, which yielded radioactive Man3GlcNAcH2. These results suggest that the mannosidase-resistant phosphorylated oligosaccharide has the structure Man leads to P leads to 6 alpha Man leads to alpha Man leads to 6 beta Man leads to 4GlcNAcH2, in which some of the phosphate groups are substituted with mannobiose instead of mannose. A second phosphorylated oligosaccharide with a mannose/phosphate ratio of 6.5 probably contains two phosphodiester groups, but its structure has not been investigated in detail.
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PMID:Carbohydrate chains on yeast carboxypeptidase Y are phosphorylated. 701 28

The toxicity to the cells and protoplasts of Saccharomyces cerevisiae of the sugar analogues modified at carbon 2 increases in the order 2-deoxy-D-glucose (DG), 2-deoxy-2-fluoro-D-glucose (FG) and 2-deoxy-2-fluoro-D-mannose (FM). The fluorohexoses, similarly as DG, behave generally as analogues of both glucose and mannose, depending on the hexose used as a carbon source in the medium. Relative inhibitions of glucan and mannan synthesis in protoplasts were found to be dependent more on glucose and mannose used as the growth support than on the type of the sugar analogue. Certain degree of structural relationship of fluorohexoses to the corresponding natural hexoses was reflected in their effects on growth of intact cells. Growth on glucose was inhibited most effectively by FM, growth on mannose by FG. The data obtained support the view that the sugar analogues interfere mainly with the glucose-mannose interconversion catalyzed by hexosephosphateisomerases. A comparison of the effects of fluorohexoses and DG on the synthesis of extracellular invertase an intracellular alpha-glucosidase and alkaline phosphatase in protoplasts pointed to the fact that all three sugar analogues tested also participate in metabolic control of enzyme synthesis.
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PMID:A comparison of the toxic effects of 2-deoxy-D-glucose and 2-deoxy-2-fluoro-D-hexoses on Saccharomyces cerevisiae cells and protoplasts. 703 85

Glycoproteins that contain phosphohexosyl groups were found to be present in the myelin- and synaptosomal-enriched fractions as well as in the microsomes of rat brain. The kinetics of flow of intraperitoneally injected [32P]phosphate suggests that the phosphate is enzymatically added in structures found in the microsomal fraction. The newly synthesized phosphoglycoproteins then appear in the soluble fraction of the synaptosomes and in the cytosol, prior to incorporation into the membranes of the synaptosomes and myelin. Phosphoglycopeptides recovered from the phosphoglycoprotein contain 3 Mannose units per N-acetylglucosamine residue; one of the mannose residues is phosphorylated. [13C]NMR studies indicate that the phosphoglycopeptides contain a chitobiose group and more than four sugar residues. Thus, the phosphomannoglycopeptides from rat brain contain an average of 2 N-acetylglucosamine, 6 mannose, and two phosphate moieties per oligosaccharide chain. Enzymatic treatment with alpha-mannosidase failed to remove the phosphomannose, although some mannose residues were released. Thus, the phosphorylated mannose is not removed by the glycosidase and terminal nonphosphorylated mannose residues are present in the oligosaccharide. The phosphate residues are removed by treatment with alkaline phosphatase.
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PMID:The metabolism and structure of phosphoglycoproteins in rat brain. 715 76

Ligatin, a receptor that recognizes phosphorylated sugars, was isolated from plasma membranes of mouse macrophages, rat ileum, and rat brain. Several acidic hydrolases including N-acetyl beta-D-glucosaminidase (beta-NAG) were solubilized with this receptor. The solubilized beta-NAG bound to ligatin in vitro as demonstrated by affinity chromatography using the immobilized receptor. beta-N-Acetyl D-glucosaminidase-ligatin complexes were dissociated by low concentrations of mannose 6-phosphate (Man6P) and/or glucose 1-phosphate (Glc 1P). The effectiveness of these two phosphomonosaccharides varied depending on the source of the enzyme: ileal beta-NAG-ligatin complexes showed a four-fold preferential dissociation with Man6P; macrophage complexes showed a 160-fold preferential dissociation with Glc 1P. Brain complexes dissociated with nearly equal preference for Man6P and Glc 1P. Heterologous complexes displayed the specificity characteristic of the source of the enzyme regardless of the source of the ligatin. Treatment of the solubilized hydrolases with endoglucosaminidase H released phosphorous-32 label from these enzymes and prevented binding of beta-NAG to ligatin. However, treatment of the solubilized hydrolases with alkaline phosphatase reduced the binding of beta-NAG to ligatin by no more than 30%. This apparent resistance of beta-NAG to dephosphorylation was consistent with the chromatographic behavior of QAE of 3H-labeled acidic oligosaccharides isolated from the solubilized hydrolases. The oligosaccharides that contain phosphorylated hexose were less acidic than phosphomonoesters and were insensitive to alkaline phosphatase until subjected to acid hydrolysis. These results suggested the presence of a phosphodiester on beta-NAG analogous to the NAC glucosamine 1 P6 mannose present on beta-glucuronidase isolated from mouse lymphoma cells (Tabas I, Kornfield, S: J Biol Chem 255: 6633, 1980).
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PMID:Ligatin binds phosphohexose residues on acidic hydrolases. 729 41

Different methods for covalent linkage of phenylboronic acid (PBA) to structural proteins and enzymes are presented. Protein-PBA conjugates, free in solution or immobilised on magnetizable polymer particles, were tested for their binding of D-sorbitol, D-mannose and glycohemoglobin (GHb). Similarly, alkaline phosphatase-PBA conjugates were used in an attempted enzyme-linked sorbent assay for the detection of GHb. Affinity chromatography on immobilised D-mannose and gel chromatographic studies of protein-PBA complexes with [14C]sorbitol, clearly illustrated a low affinity of the interaction studied. Glycated hemoglobin could not be detected using the enzyme-linked sorbent assay approach. However, GHb was found to be specifically retained on columns filled with protein-PBA-coated particles as affinity matrix, enabling the glycation level of blood samples to be determined.
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PMID:Protein-boronic acid conjugates and their binding to low-molecular-mass cis-diols and glycated hemoglobin. 749 83

Strains of a new species, Staphylococcus vitulus, were isolated from food and a variety of mammals. This species was recognized on the basis of the results of an analysis of genomic EcoRI fragments containing portions of the rRNA operons. The patterns of hybridized fragments obtained from strains belonging to the new taxon were sorted into a distinguishable cluster and were distinct from the Staphylococcus lentus and Staphylococcus sciuri patterns. The results of DNA-DNA hybridization reactions demonstrated that strains in this cluster were more closely related to S. lentus and S. sciuri than to other Staphylococcus species and yet were significantly different. While these strains had some of the phenotypic characteristics of the S. sciuri species group, the newly recognized taxon could be distinguished by its very small colonies on P agar, absence of alkaline phosphatase activity, and lack of acid production from L-arabinose, maltose, N-acetylglucosamine, D-mannose, and raffinose. The type strain of the new species is strain DD 756 (= ATCC 51145).
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PMID:Identification of the Staphylococcus sciuri species group with EcoRI fragments containing rRNA sequences and description of Staphylococcus vitulus sp. nov. 752 Jul 36

Ascorbic acid is necessary for expression of the osteoblast phenotype. We examined whether Na(+)-dependent transport is required for MC3T3-E1 preosteoblast cells to respond to vitamin C and investigated the role of membrane transport in the intracellular accumulation and function of ascorbate. MC3T3-E1 cells were found to possess a saturable, stereoselective, Na(+)-dependent ascorbic acid transport activity that is sensitive to the transport inhibitors sulfinpyrazone, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, and phloretin. Transport activity showed no competition with glucose or 2-deoxyglucose and was not inhibited by cytochalasin B, indicating that it is distinct from known hexose transporters. On addition of 100 microM ascorbic acid to the extracellular medium, intracellular concentrations of 10 mM were reached within 5-10 h and remained constant for up to 24 h. A good correlation was observed between intracellular ascorbic acid concentration and rate of hydroxyproline synthesis. Although ascorbic acid was transported preferentially compared with D-isoascorbic acid, both isomers had equivalent activity in stimulating hydroxyproline formation once they entered cells. Marked stereoselectivity for extracellular L-ascorbic acid relative to D-isoascorbic acid was also seen when alkaline phosphatase and total hydroxyproline were measured after 6 days in culture. Moreover, ascorbic acid transport inhibitors that prevented intracellular accumulation of vitamin blocked the synthesis of hydroxyproline. Thus Na(+)-dependent ascorbic acid transport is required for MC3T3-E1 cells to achieve the millimolar intracellular vitamin C concentrations necessary for maximal prolyl hydroxylase activity and expression of the osteoblast phenotype.
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PMID:Requirement for Na(+)-dependent ascorbic acid transport in osteoblast function. 761 63


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