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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chemical composition and serological activity of free lipid A from Proteus were studied. Only two fatty acids: myristic acid and 3-hydroxymyristic acid were detected. When calculated for glucosamine disaccharide unit, 2 moles of ester-linked and 1 mole of amide-linked fatty acid are present. Amino group of glucosaminyl residue is substituted by 3-hydroxymyristic acid. The occurence of an uncommon (4-aminoarabinose) substituent, attached outside the backbone, was noticed. The results of serological investigation indicate the great similarity between antigenic determinants of Proteus lipid A and Salmonella-type of lipid.
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PMID:Immunochemical studies on free lipid A from Proteus mirabilis 1959. 37 79

A glucose-binding glycoprotein (GBP) from the periplasm of Pseudomonas aeruginosa was purified to homogeneity as judged by polyacrylamide gel electrophoresis, molecular sieve chromatography, and double-diffusion gel precipitation. It had an average molecular weight of 44,500 and an isoelectric point of 4.7. One mole of glucose was bound per mole of GBP with a dissociation constant of 0.35 muM. The binding of radioactive glucose by GBP was not significantly inhibited by 10-fold-higher concentrations of other carbohydrates; however, a number of related compounds were found to compete at 100-fold-higher concentrations. Amino acid analyses revealed predominant amounts of alanine, glutamate, and glycine and a low content of sulfur-containing amino acids. The carbohydrate moiety of GBP, comprising nearly 16% of the total weight, contained galactosamine, glucosamine, fucose, galactose, glucose, and mannose. A GBP-deficient mutant, strain MB723, was found to be defective in both membrane transport and glucose chemotaxis. Strain MB724, a revertant to GBP-positive phenotype, simultaneously recovered normal levels of both membrane functions.
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PMID:Purification and properties of the periplasmic glucose-binding protein of Pseudomonas aeruginosa. 40 16

Beta-conglycinin consisting of six major isomers (designated B1- to B6-conglycinin) was dissociated and fractionated on columns of DEAE- and CM-Sephadex in buffers containing 6 M urea. Three major (alpha, alpha' and beta) and one minor (gamma) subunits were isolated and further characterized by gel electrophoresis and gel electrofocusing. Gel electrophoresis in urea and in sodium dodecyl sulfate, and gel filtration in 6 M guanidine hydrochloride gave a molecular weight of 57 000 for alpha, alpha' subunits; and 42 000 for beta and gamma subunits. The isoelectric points of the isolated subunits, measured by disc gel electrofocusing, were as follows: alpha, 4.90; alpha', 5.18; beta, 5.66-6.00. On gel electrofocusing, beta subunit showed four microheterogeneous components; three of them comprised 95% of the total beta subunit. Leucine and valine were the N-terminal amino acids of beta and alpha alpha' subunits, respectively. The isolated subunits contained mannose and glucosamine in varying quantities. Two carbohydrate moieties were calculated for one mole of alpha, alpha' subunits; and one carbohydrate moiety for the beta subunit. Considerable similarity in the amino acid composition of alpha and alpha' subunits was observed. The beta subunit was devoid of cysteine and methionine; and in comparison with alpha, alpha' subunits, had a higher content of hydrophobic amino acids. The isolated subunits exhibited antigen-antibody reaction with antisera to the native beta-conglycinin. Each of them was partglycinins. The alpha and alpha' subunits were in addition identical with each other and with B5-, B6-conglycinins. They were immunologically unrelated with beta subunit. The recovery of immuno-properties from the individual subunits may be attributed to the reconstruction of the three-dimensional structure upon removal of denaturing reagents.
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PMID:Beta-conglycinin from soybean proteins. Isolation and immunological and physicochemical properties of the monomeric forms. 55 58

The carbohydrate of variant-specific surface antigen glycoproteins from bloodstream forms of 13 cloned variants of Trypanosoma brucei was analyzed by gas-liquid chromatography. The glycoproteins contained from 6 to 17% carbohydrate by weight, and all contained the same 4 sugars: mannose, galactose, glucose, and glucosamine (probably as N-acetylglucosamine). The glycoprotein from variant 048, strain 427 contained (+20%) 11 mannose, 4 galactose, 4 glucose, and 5 glucosamine residues/mole of glycoprotein (molecular weight 65,000). Glucose was an intergral component of the glycoproteins, not dissociable by sodium dodecyl sulphate, 8 M urea, or 1 M acetic acid. Some of the glucose was dissociated by trichloroacetic acid. Most of the glycoproteins formed precipitin with concanavalin A in Ouchterlony double diffusion, but none formed such bands with wheat germ agglutinin or Ricinus communis lectin (molecular weight 120, 000).
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PMID:Carbohydrate composition of variant-specific surface antigen glycoproteins from Trypanosoma brucei. 59 4

The purified ricinotoxin from Ricinus communis L. seeds appears to be a glycoprotein. Either paper or gas-liquid chromatographic methods indicate that only mannose and N-acetyl-glucosamine are present in significant amounts. Quantitative determination shows that one mole of ricinotoxin contains 15 mannose residues and 8 N-acetyl-glucosamine residues.
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PMID:Characterization, composition and determination of the sugars in ricinotoxin from Ricinus communis L. seeds. 74 70

Characterization of glycopeptides obtained on alkaline hydrolysis and on extensive collagenase and pronase digestion of the intestinal basement membrane showed the existence of two distinctly different carbohydrate units. One of these is a disaccharide, composed of glucose and galactose, linked to hydroxylysine. It was shown to be identical to the unit (2-O-D-glucopyranosyl-O-D-galactopyranosylhydroxylyasine) present in vertebrate basement membranes, as determined from stability to alkaline hydrolysis, retention time on amino acid analyzer, chemical composition, graded acid hydrolysis, methylation analysis, and periodate oxidation. Direct quantitation after alkaline hydrolysis showed the presence of 9.71 disaccharide units/1000 amino acid residues, indicating that 89% of the hydroxylysine residues of the intestinal membrane are glycosylated. The other unit, consisting of the remaining monosaccharides of the membrane, was separated from the disaccharide unit by gel filtration and ion exchange chromatography of collagenase/pronase digests. Chemical analyses and molecular weight determination by thin layer gel filtration chromatography of purified glycopeptides indicated that this unit is an oligosaccharide which is composed of fucose, galactose, mannose, galactosamine, and glucosamine in a mole ratio of 1:1:1:1:2, respectively. The amount of this unit was calculated to be 2.6 units/1000 amino acid residues.
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PMID:Intestinal basement membrane of Ascaris suum. Characterization of carbohydrate units. 86 12

Four major glycoproteins were extracted by dilute salt solution from procine mitral valvular tissue. Two of these major glycoproteins, procine valve glycoprotein I and porcine valve glycoprotein III, were isolated and purified by fractionation of salt extract with ammonium sulfate followed by column chromatography on DEAE-cellulose. The purified glycoproteins appeared to be homogeneous by polyacrylamide disc electrophoresis in several buffer systems, and by Sephadex filtration. The porcine valve glycoprotein I has a molecular weight of approximately 120000. Isoelectric focusing yielded a single band, pI = 5.8. The glycoprotein contained large amounts of acidic amino acids, and amide nitrogen. The carbohydrate moiety was composed of fucose, mannose, galactose, glucose, glucosamine, and galactosamine in the molar ratio of 5:10:15:12:7:2 per mole of glycoprotein. The second major glycoprotein, porcine valve glycoprotein III, has an approximate molecular weight of 72000. This glycoprotein gives two bands upon analytical isoelectric focusing with isoelectric points of pI = 4.1 and 4.3. Porcine valve glycoprotein III contained large amounts of acidic amino acids and low amounts of amide nitrogen. Its carbohydrate moiety was composed of glucose, galactose, mannose, fucose, glucosamine, and sialic acid in the ratio of 3:3:2:1:4:1 mol/mole of glycoprotein. This glycoprotein was similar to a glycoprotein preparation isolated from porcine aortic intima by P.V. Wagh and B.I. Roberts (1972), Biochemistry 11, 4222.
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PMID:Purification and chemical characterization of salt-extractable glycoproteins from porcine mitral valve. 93 28

The glucose transport system in Leishmania tropica promastigotes was characterized by the use of labeled 2-deoxy-D-glucose (2-DOG), a nonmetabolizable glucose analog. The uptake system has a Q10 of 2 and a heat of activation of 10.2 kcal/mole. The glucose transport system is subject to competitive inhibition by 2-DOG, glucosamine, N-acetyl glucosamine, mannose, galactose, and fructose which suggests that substitutions in the hexose chain at carbons 2 and 4 do not affect carrier specificity. In contrast, changes at carbon 1 (alpha-methyl-D-glucoside, 1,5-anhydroglucitol) and carbon 3 (3-0-methyl glucose) lead to loss of carrier affinity since these sugars do not compete for the glucose carrier. Sugars that compete with the glucose carrier have one common feature--they all exist in the pyranose form in solution. The carrier for D-glucose does not interact with L-glucose or any of the pentose sugars tested. Uptake of 2-DOG is inhibited by glycerol. This inhibition, however, is noncompetitive; it is evident; therefore, that glucose and glycerol do not compete for the same carrier. Glycerol does not repress the glucose carrier since cells grown in presence of glycerol transport the sugar normally.
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PMID:Specificity of the glucose transport system in Leishmania tropica promastigotes. 97 53

Transcobalamin I and transcobalamin III have been purified approximately 6,000,000- and 3,000,000-fold, respectively, from normal human plasma using a purification scheme consisting of immunoadsorption, dialysis against 7.5 M guanidine HCl to remove endogenous vitamin B12, and affinity chromatography on vitamin B12-Sepharose. The two proteins were separated from each other subsequently by chromatography on DEAE-cellulose. The vitamin B12-binding protein present in granulocytes obtained from normal subjects has been purified approximately 5000-fold using affinity chromatography on vitamin B12-Sepharose as the sole purification technique. The final preparations of all three proteins were homogeneous based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Transcobalamin I and transcobalamin III belong to the R-typed class of vitamin B12-binding proteins and are indistinguishable from each other, and from the human granulocyte, milk, and saliva R-type vitamin B12-binding proteins, when studied by immunodiffusion with rabbit anti-human milk vitamin B12-binding protein sera. The carbohydrate compositions, expressed as moles of carbohydrate per mole of vitamin B12, of transcobalamin I, transcobalamin III, and the normal granulocyte vitamin B12-binding protein, respectively, are: sialic acid, 18, 11, 11; fucose, 9, 20, 24; galactose, 41, 51, 46; mannose, 24, 22, 20; galactosamine, 2, 2, 2; and glucosamine, 46, 54, 46. The high sialic acid content of transcobalamin I appears to account for the fact that this protein elutes after transcobalamin III and the normal granulocyte vitamin B12-binding protein during chromatography on DEAE-cellulose. This observation provides support for the hypothesis that differences among the R-type vitamin B12-binding proteins are due to differences in carbohydrate content. The similarities in carbohydrate composition and other properties of transcobalamin III and the granulocyte vitamin B12-binding protein provide support for the hypothesis that human plasma transcobalamin III is derived from granulocytes. The differences observed between transcobalamin I and the normal granulocyte vitamin B12-binding protein suggest that transcobalamin I may not be derived from granulocytes.
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PMID:Human plasma R-type vitamin B12-binding proteins. I. Isolation and characterization of transcobalamin I. TRANSCOBALAMIN III. and the normal granulocyte vitamin B12-binding protein. 117 44

Sialoproteins isolated from the soluble fraction of rat liver could be incorporated into microsomal membranes. This incorporation was dependent on protein concentration, time, and temperature. Sodium dodecyl sulfate gel electrophoresis of membrane proteins after in vitro incorporation showed four major sugar-containing peaks and was similar to that found after in vivo labeling. Most of the incorporated protein was tightly bound to the microsomal membrane. Gel filtration and ion-exchange chromatography revealed the presence of several cytosolic glycoproteins that could be incorporated into microsomes. During prolonged centrifugation in a KBr solution with a density of 1.21 a highly labeled ([3H]glucosamine) protein (mole wt approximately to 70,000) that was actively incorporated into microsomes could be recovered in the upper region of the tube. These results demonstrate that several cytoplasmic glycoproteins of rat liver are transferred into microsomal membranes and that one of these is a lipoprotein.
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PMID:Biogenesis of microsomal membrane glycoproteins in rat liver. II. Purification of soluble glycoproteins and their incorporation into microsomal membranes. 120 19


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