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)

Obese patients (44) were studied on a 320 kcal diet for one to two months. No ECG changes were seen in 43 patients. One patient showed a transient T wave inversion after six weeks dieting, but the significance of this finding is doubtful. We have found a 320 kcal formula diet a safe and effective method of out-patient weight reduction with no patient showing any ECG abnormality in the first four weeks of dieting. ECGs and medical supervision are recommended for patients maintained on low-calorie diets for periods longer than a month. Nitrogen balance reached equilibrium in five to six weeks. Biochemical estimations showed minor changes such as falls in the serum cholesterol and rises in the alkaline phosphatase and bilirubin, but no clinically important changes were observed. One patient on propranolol for hypertension developed postural hypotension and required substantial reduction of medication.
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PMID:Low-calorie-formula diets--are they safe? 727 63

Substrates commonly used for localizing bone Golgi apparatus (GA) acid phosphatase (AcPase), e.g., beta-glycerophosphate, p-nitrophenylphosphate, cytidine-5'-monophosphate, and di(dicyclohexylammonium)-2-napthylthiolphosphate, give strong staining not only of GA but also of lysosomes. Thiamine pyrophosphate and inosine-5'-monophosphate--substrates that give good GA staining in some soft tissues--give only lysosomal staining in bone. No previously used substrate or substrate-effector combination has selectively localized the GA acid phosphatase in bone. This article describes results using a new AcPase medium having pyridoxal-5'-phosphate (PLP) as substrate. In bone this medium produced strong staining of the osteoblast GA, but relatively little staining of lysosomes, including lysosomes in osteoclasts. The weak lysosomal staining was almost totally eliminated, without affecting the GA reaction, by pretreating the tissue in 0.3% NH3 solution. Conversely, elevated ionic strength of the substrate medium eliminated the GA reaction, while having little effect on lysosomal staining. The GA enzyme was very sensitive to 1 mM tartrate whereas the lysosomal enzyme was not. These differences suggest the presence of distinct isoenzymes in the two locations. The distribution of osteoblasts with stained GA coincided with the distribution of strongest alkaline phosphatase activity and rapid bone mineralization, supporting previous suggestions that osteoblast GA AcPase is involved in the processing of one or more newly synthesized bone matrix components.
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PMID:Selective localization of a Golgi apparatus acid phosphatase isoenzyme in bone using pyridoxal-5'-phosphate. 735 10

A histochemical investigation has been made to localize and characterize various lipid, protein, carbohydrate and enzyme constituents present within the different cell types of the epidermis of Anabas testudineus. The polygonal cells contain glycogen, the amount of which gradually increases as the cells move towards the surface until they reach the most superficial layer where the amount of glycogen slightly decreases indicating the metabolically active state of these cells. The basal cells, which frequently undergo cell proliferation, contain no glycogen. The polygonal cells give strong reactions for SDH, alkaline phosphatase, cholesterol esters and nonsulphated acid mucopolysaccharides, moderate reactions for acidic lipids, phospholipids and free cholesterol and weak reactions for neutral mucopolysaccharides, protein bound NH2 groups, mucoprotein, tyrosine, tryptophan and cysteine bound sulphydryl groups. These cells in the outermost layer give stronger reactions for acidic lipids, phospholipids and cholesterol esters and weaker reactions for SDH and alkaline phosphatase activities. The above findings reveal that the polygonal cells remain metabolically active throughout the epidermis. The mucous cells are numerous and secrete mixture of neutral mucopolysaccharides, sulphated acid mucopolysaccharides and nonsulphated acid mucopolysaccharides. The contents of the sacciform granulated cels are mainly proteins. A thick coat of slime over the body surface containing mucopolysaccharides, lipids and proteins is important in keeping the skin moist and may facilitate the survival of the fish while it is on land. The melanophores in the epidermis may playing important role in preventing the colinization by parasites, fungi and bacteria over the body surface, act as macrophages.
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PMID:A histochemical study of the epidermis of the climbing perch, Anabas testudineus (Anabantidae, Pisces). 742 82

We have purified and characterized recombinant Xenopus bone morphogenetic proteins (xBMPs): homodimers of xBMP-4, 7 and heterodimers (xBMP-4/7) produced by a baculovirus expression system. Highly purified xBMPs had homogeneous NH2-termini predicted from a consensus motif, Arg-X-X-Arg, while they possessed diverse sugar chains. Implantation of xBMPs together with pure collagen carrier in rats induced new bone formation in a dose-dependent manner. The xBMP-4/7 heterodimer showed the strongest activity, with an effective dose of 1-30 micrograms, while more than 10 micrograms of xBMP-4 or 7 homodimer was required for a significant effect. Histological examination revealed that xBMP-4/7 implants showed intramembranous ossification without chondrogenesis. In primary cultures of rat bone marrow stromal cells, xBMP-4/7 induced alkaline phosphatase 3-fold more strongly than xBMP-7 and 20-fold more than xBMP-4. These results suggest that the heterodimeric form of BMP would generate the strongest signal triggering osteogenic differentiation of osteoprogenitor cells in adult tissues.
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PMID:Potent ectopic bone-inducing activity of bone morphogenetic protein-4/7 heterodimer. 776 40

The effects of fortification of preterm human milk were evaluated by comparing two groups of very low birth weight infants (birth weight < or = 1300 g, gestational age < or = 30 weeks): six fed preterm human milk fortified with a commercially available protein-mineral supplement (protein 0.7 g/dl, calcium 90 mg/dl, phosphorus 45 mg/dl) and seven fed unfortified preterm human milk. Nitrogen and energy balance studies were performed at an average age of 56 postnatal days. Nitrogen retention in the fortified group (348.2 +/- 70.5 mg/kg/day) was significantly greater than that in the unfortified group (196.0 +/- 50.0 mg/kg/day) and similar to that of fetuses of comparable gestational age. Energy stored by the two groups did not differ. At age 8 weeks, the infants in the fortified group had higher serum protein, higher serum albumin, and better mineral status (higher serum calcium and phosphorus and lower alkaline phosphatase and renal tubular reabsorption of phosphate). The bone density and width of the distal third radius, as measured by X-ray microdensitometry, were greater in the fortified group than in the unfortified group 12 weeks after birth. These results suggest that the supplement corrects any nutritional inadequacies of preterm human milk for very low birth weight infants.
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PMID:Nutrient balance, metabolic response, and bone growth in VLBW infants fed fortified human milk. 784 42

A method is described for Western blotting of peptides as small as 400 daltons (Da). Peptides were separated by tricine-sodium dodecyl sulfate electrophoresis and electroblotted to gelatin-coated PH79 nitrocellulose paper (0.1 micron). The electroblotted peptides were fixed to the nitrocellulose paper for 5-10 min in 4% paraformaldehyde solution. Using anti-rabbit FMRF-amide (Phe-Met-Arg-Phe-NH2) as primary antibody, positive immunoreactivity was detected with an amplified alkaline phosphatase assay which was sensitive to at least 0.5 microgram FMRFamide/lane. When immunoreactivity was determined with 125I-protein A, it was possible to amplify and detect weak signals by increasing the autoradiography time. Therefore, using the 125I-protein A detection method, Western blot analysis of brain extracts from Lymnaea stagnalis (pond snail) and Poecilia reticulata (guppy) indicated the presence of four FMRFamide immunoreactive bands after a 7-day exposure to X-ray film. The most abundant peptide coelectrophoresed with the FMRFamide standard (M(r) 598.8 Da). In addition, this Western blotting procedure also detected APGWamide (Ala-Pro-Gly-Try-NH2; 428.5 Da) and [D-Ala2]-Leu-enkephalinamide (568.7 Da) with their respective specific antibodies.
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PMID:Western blotting of formaldehyde-fixed neuropeptides as small as 400 daltons on gelatin-coated nitrocellulose paper. 791 87

Addition of a nitrogen-source to glucose-repressed, nitrogen-starved G0 cells of the yeast Saccharomyces cerevisiae in the presence of a fermentable carbon source induces growth and causes within a few minutes a five-fold, protein-synthesis-independent increase in the activity of trehalase. Nitrogen-activated trehalase could be deactivated in vitro by alkaline phosphatase treatment, supporting the idea that the activation is triggered by phosphorylation. Yeast strains containing only one of the three TPK genes (which encode the catalytic subunit of cAMP-dependent protein kinase) showed different degrees of nitrogen-induced trehalase activation. The order of effectiveness was different from that previously reported for glucose-induced activation of trehalase in glucose-depressed yeast cells. Further reduction of TPK-encoded catalytic subunit activity by partially inactivating point mutations in the remaining TPK gene further diminished nitrogen-induced trehalase activation, while deletion of the BCY1 gene (which encodes the regulatory subunit) in the same strains resulted in an increase in the extent of activation. Deletion of the RAS genes in such a tpkw1 bcy1 strain had no effect. These results are consistent with mediation of nitrogen-induced trehalase activation by the free catalytic subunits alone. They support our previous conclusion that cAMP does not act as second messenger in this nitrogen-induced activation process and our suggestion that a novel nitrogen-induced signaling pathway integrates with the cAMP pathway at the level of the free catalytic subunits of protein kinase A. Western blot experiments showed that the differences in the extent of trehalase activation were not due to differences in trehalase expression. On the other hand, we cannot completely exclude that protein kinase A influences the nitrogen-induced activation mechanism itself rather than acting directly on trehalase. However, any such alternative explanation requires the existence of an additional, yet unknown, mechanism for activation of trehalase besides the well-established regulation by protein kinase A.
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PMID:Activation of trehalase during growth induction by nitrogen sources in the yeast Saccharomyces cerevisiae depends on the free catalytic subunits of cAMP-dependent protein kinase, but not on functional Ras proteins. 799 5

Various sensor technologies require a monolayer of tightly bound proteins. Five methods for protein immobilization were evaluated, comprising two methods of linker attachment to a silicon nitride surface (CNBr, silanization) and three methods of linker attachment to the protein (via primary amines, carboxyl groups, and the aromatic rings of tyrosine and histidine). These covalent binding methods were evaluated by immobilization of the enzyme alkaline phosphatase and with monoclonal antibodies tagged with 125I. It was determined that approximately 75% of the protein on the "covalently" immobilized samples was simply adsorbed. Adsorption was reduced by varying the pH and ionic strength of the wash buffers as well as by adding chaotropes and competitors to the wash buffer. A more efficient method of reducing adsorption was to perform the immobilization in the presence of a detergent; 0.5% Tween 60 was the most effective detergent studied. The optimized procedure gives a surface loading of 1.20 x 10(12) MAb/cm2. of which approximately 10% was adsorbed protein. This surface density is consistent with a monolayer of immobilized protein. This protein was shown to be active by challenging immobilized antibodies with 35S-labelled antigen; only the antibody/antigen pair released radioactive material upon elution.
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PMID:Covalent immobilization of protein monolayers for biosensor applications. 801 17

Glycosyl-phosphatidylinositol-anchored membrane proteins (GPI-proteins) are normally identified either by cleavage of the lipid anchor using (glycosyl)phosphatidylinositol-specific phospholipases C or D (GPI-PLs) or by metabolic labeling of the lipid moiety with specific building blocks. Therefore, methods for discrimination between transmembrane proteins and GPI-proteins on the basis of their physicochemical properties are desirable. Here we are presenting a selective extraction method for typical well-characterized mammalian GPI-proteins, e.g., acetylcholine esterase, alkaline phosphatase, 5'-nucleotidase, and lipoprotein lipase, using a derivative of taurocholate. The results were compared to those obtained with well-characterized transmembrane proteins, e.g., insulin receptor and hydroxymethyl glutaryl coenzyme A-reductase, glucose transporters, or aminopeptidase M and several commercially available detergents. With regard to total membrane proteins, it was possible to selectively enrich GPI-proteins up to 8- to 14-fold by using concentrations between 0.1 and 0.3% of 4'-NH2-amino-7 beta-benzamido-taurocholic acid (BATC). In addition, the cleavage specificity and efficiency of (G)PI-PLs were increased in the presence of identical concentrations of BATC compared to commonly used detergents, e.g., Nonidet P-40. Therefore, the present study shows that the use of BATC facilitates the identification of glycosyl-phosphatidylinositol-anchored membrane proteins.
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PMID:4'-Amino-benzamido-taurocholic acid selectively solubilizes glycosyl-phosphatidylinositol-anchored membrane proteins and improves lipolytic cleavage of their membrane anchors by specific phospholipases. 813 45

Cytochromes P450 are inserted into and anchored to the endoplasmic reticulum (ER) membrane by a hydrophobic signal sequence at the NH2 terminus. To determine whether the NH2-terminal sequence might also have an ER retention function, the NH2-terminal 29 amino acids of cytochrome P450 2C1, with and without an additional 29 amino acids containing an N-glycosylation site, were fused either to a soluble cytoplasmic protein, Escherichia coli beta-galactosidase, or to a secreted protein, E. coli alkaline phosphatase, and the hybrid proteins were expressed in COS1 cells. Subcellular fractionation indicated that both the beta-galactosidase and alkaline phosphatase hybrid proteins cosedimented with marker enzymes for ER membranes, and localization by immunofluorescent staining was consistent with an ER location. Hybrid proteins with the NH2-terminal glycosylation site were glycosylated in COS1 cells, and the carbohydrate moiety was sensitive to endoglycosidase H digestion, providing further evidence that the proteins were retained in the ER. In vitro studies of membrane insertion of the alkaline phosphatase hybrid indicated that fusion to alkaline phosphatase hybrid indicated that fusion to alkaline phosphatase did not alter the topological properties of the cytochrome P450 NH2-terminal sequence. In addition, alkaline phosphatase fused to the extracellular and transmembrane domains of epidermal growth factor receptor was transported to the plasma membrane in COS1 cells, which establishes that alkaline phosphatase as a cytoplasmic domain does not prevent transport from the ER. These observations indicate that the large cytoplasmic domain of cytochrome P450 is not required for retention in the ER and suggest that a specific sequence or structure within the NH2-terminal 29 amino acids functions as an ER retention signal.
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PMID:The amino-terminal 29 amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum. 836 Jan 66


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