Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cell walls were isolated by mechanical disruption of mid-log phase cells of Bacillus stearothermophilus NCA 1503-4R grown in Trypticase-yeast extract-fructose medium at 55 C. The cell walls were purified by treatment with sodium dodecyl sulfate (SDS) and incubation with deoxyribonuclease and trypsin. The cell wall peptidoglycan contained glucosamine, muramic acid, alpha, epsilon-diaminopimelic acid, and glutamic acid. Low amounts of glycine, galactosamine, serine, aspartic acid, lysine, and valine were also present. The relative mole ratios of glutamic acid-alpha, epsilon-diaminopimelic acid-glycine-alanine were 1.00:1.26:0.08:1.55. The cell walls were free from ribonucleic acid and deoxyribonucleic acid and contained less than 0.2% chloroform-methanol extractable lipid and 0.09 mumole of phosphorus per mg of cell wall. Teichoic acid was not detected in the cell walls of this organism. Cell walls isolated without treatment with SDS contained 7.5% chloroform-methanol extractable lipid, 0.24 mumole of phosphorus per mg of cell wall, and relatively high concentrations of all amino acids. These results suggest that the extracted lipid is not a cell wall component per se, but a contaminant from the lipoprotein cell membrane.
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PMID:Chemical composition of the cell walls of Bacillus stearothermophilus. 603 16

A photoaffinity analogue of UDP-galactose, 4-azido-2-nitrophenyluridylyl pyrophosphate (ANUP), has been synthesized for the investigation of the binding topography of alpha-lactalbumin on galactosyltransferase. Results obtained from steady state kinetics show that ANUP is an effective competitive inhibitor against UDP-galactose in the reactions of lactose and N-acetyllactosamine syntheses. The specific binding of ANUP to the UDP-galactose-binding site is further demonstrated by its ability to facilitate the formation of the lactose synthase complex on solid supports, either alone or in the presence of glucose or N-acetyl-glucosamine. ANUP inactivates galactosyltransferase on irradiation. One mole of ANUP was incorporated per mol of enzyme inactivated. This process is Mn2+-dependent and can be prevented by UDP-galactose. Glucose and N-acetylglucosamine render only partial protection. Photoaffinity labeling of lactose synthase either free in solution or immobilized on Sepharose does not result in any reduction of the alpha-lactalbumin modifier activity. In addition, no incorporation of radioactivity into alpha-lactalbumin was observed when radioactive ANUP was used, whereas galactosyltransferase was labeled. These data indicate that alpha-lactalbumin does not bind to galactosyltransferase in the region of the ANUP site, suggesting that the location of protein-protein interaction between the two subunits of lactose synthase may be removed from the UDP-galactose-binding domain.
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PMID:Photoaffinity labeling of lactose synthase with a UDP-galactose analogue. 641 60

We compare the complete carbohydrate composition of IgG purified from the serum of patients with cystic fibrosis (CF) with that of control subjects. Our results indicate that IgG from cystic fibrosis patients is underglycosylated with respect to galactose and sialic acid, the two terminal sugars on the antennae of the complex-type oligosaccharide chains found on IgG. The galactose content, as determined by gas liquid chromatography, was 2.81 +/- 0.86 (S.D.) mole/mole of IgG for normal subjects versus 1.5 +/- 0.39 for CF subjects (P less than 0.025). Sialic acid content, as determined by the Warren procedure, was 1.33 +/- 0.39 for normals versus 0.47 +/- 0.10 for CF subjects (P less than 0.001). Neither galactose nor sialic acid values for the two groups overlapped. The contents of the core sugars, mannose and glucosamine, and of fucose were not significantly different. When the data are expressed as residues per 3 moles mannose, similar results are obtained. We suggest that immune complex formation, which has been documented in many CF patients, exposes sugar chains of IgG molecules to hydrolytic activity of serum glucosidases, resulting in partial removal of the more peripheral sugars. Because serum glycoproteins missing sialic acid and galactose are not readily cleared from the circulation, the observed changes may contribute to elevated levels of IgG and immune complexes in older people with CF.
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PMID:The carbohydrate content of IgG from patients with cystic fibrosis. 665 24

A procedure for the isolation of the human complement (C) protein C9 is described. The procedure allowin. The purified protein has the electrophoretic mobility of an alpha-globulin, and is a single polypeptide chain with a m.w. of 71,000. No impurities were detected either on gel electrophoretic or immunochemical examination. C9 is a glycoprotein containing 7.8% carbohydrate, and in terms of residues per mole, 3.0 glucosamine, 17.6 neutral hexose, and 7.4 sialic acid. Its amino acid composition is typical of a globular serum protein. Upon automated Edman degradation of reduced and alkylated C9, no amino acid residues were released, suggesting a blocked N-terminus. The concentration of C9 in normal human serum is 58 +/- 8 microgram/ml. A high titer rabbit antiserum was produced and employed to immunochemically deplete serum of C9. The CH50 of the C9-depleted serum was identical to that of whole human serum; however, membrane fragments of erythrocytes lysed by C9-depleted serum lacked the typical ultrastructural C lesions, which constitute the dimeric membrane attack complex.
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PMID:The ninth component of human complement: purification and physicochemical characterization. 676 71

Glycosaminoglycan isolated from urine of a patient with the Hurler-Scheie compound syndrome consisted of dermatan sulfate (60%), heparan sulfate (34%) and chondroitin sulfate (6%). About 60% of both dermatan and chondroitin sulfates had molecular weight 8,000-10,000, while 95% of the heparan sulfate had molecular weight less than 6,000. The total sulfate content of the glycosaminoglycans increased with decrease in molecular weight. N-sulfate content in the heparan sulfate, however, had no relation to molecular weight, and was 0.33 mole per mole of glucosamine on the average. About 70% of the heparan sulfate with the lowest molecular weight (1,500) were composed of three repeating disaccharide units of heparan sulfate and two acetyl, one N-sulfate and three O-sulfate groups linked to the units. The dermatan sulfate contained 1.0-1.2 moles of sulfate per mole of galactosamine. Of the excess sulfate 45-65% were bound to iduronate residues and the rest to C-6 of N-acetylgalactosamine 4-sulfate residues. Most of the dermatan sulfate (83.2-100%) had nonsulfated iduronic acid at the non-reducing end. This finding is consistent with the defect of iduronidase in this disease.
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PMID:Characteristics of urinary glycosaminoglycans excreted by a patient with the Hurler-Scheie compound syndrome. 680 94

Ricin is an extremely toxic phytotoxin from the castor-oil plant seeds. This toxin is different from the two phyto-hemagglutinins or lectins which are also present in the seeds and can be purified in two chromatographic steps. Studies on the physical and chemical properties of pure ricin are given (molecular weight: 65 750 daltons, glycoproteic nature, oses composition: 15 moles of mannose and 8 moles of N-acetyl-glucosamine per mole of ricin, aminoacids composition: 545, bicatenary structure: the toxin is formed by two polypeptide A and B chains linked together by a disulfure bond). Though ricin is resistant to proteolytic enzymes under normal conditions, we have found conditions in which tryptic hydrolysis of the toxin gives several peptides which retain toxicity. Two of them were purified. The LD50 on mice of ricin and its isolated toxic peptides were determined, the symptoms of ricin's intoxication were established on animals which died from a dramatic hepatonephritic injury, but always after a lag. Ricin has a cytostatic, and then a cytotoxic effect on cells in culture which are highly damaged (important membranous protrusions). The mechanism of ricin's action was studied. It inhibits elongation in protein synthesis in vivo as well as in vitro, by acting on ribosomes whether cytoplasmic, mitochondrial or chloroplastic. To act, the ricin A-chain must be activated by ribosomes which split the ricin molecule into its polypeptide chains; these ribosomes are then frozen by the toxin and became inefficients in protein synthesis.
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PMID:[Ricin, the toxic protein of the castor-oil plant (Ricinus communis L). Structure and properties (author's transl)]. 700 33

1. A method was developed whereby [1-14C]glucosamine was used in a perfused rat liver system to prepare over 2 mg of alpha 1-acid glycoprotein with highly radioactive sialic acid and glucosamine residues. 2. The liver secreted radioactive alpha 1-acid glycoprotein over a 4-6 h period, and this glycoprotein was purified from the perfusate by chromatography on DEAE-cellulose at pH 3.6. 3. The sialic acid on the isolated glycoprotein had a specific radioactivity of 3.1 Ci/mol, whereas the glucosamine-specific radioactivity was 4.3 Ci/mole. The latter amino-sugar residues on the isolated protein were only 13-fold less radioactive than the initially added [1-14C]glucosamine. Orosomucoid with a specific radioactivity of 31.3 microCi/mg of protein was obtainable by using [6-3H]glucosamine. 4. The amino acid composition of the purified orosomucoid was comparable with that found by others for the same glycoprotein isolated from rat serum. A partial characterization of the carbohydrate structure was done by sequential digestion with neuraminidase, beta-D-galactosidase and beta-D-hexosaminidase. 5. Many other radioactive glycoproteins were found to be secreted into the perfusate by the liver. Thus this experimental system should prove useful for obtaining other serum glycoprotein with highly radioactive sugar moieties.
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PMID:Use of radioactive glucosamine in the perfused rat liver to prepare alpha 1-acid glycoprotein (orosomucoid) with 3H- or 14C-labelled sialic acid and N-acetylglucosamine residues. 710 33

Using gas-liquid and column chromatography, the carbohydrate composition of the visual protein rhodopsin from wall-eyed pollock purified by SDS-electrophoresis was studied. It was found that similar to bovine rhodopsin, the protein from wall-eyed pollock contains in its carbohydrate moiety only two types of monosaccharides, i. e. mannose and glucosamine (1,78 +/- 0,13 moles of mannose per one mole of glucosamine). One mole of rhodopsin contains 9,43 +/- 1,5 moles of mannose and 5,3 moles of glucosamine. The data obtained suggest a similarity of the carbohydrate component of wall-eyed pollock rhodopsin to that of the traditional object--bovine rhodopsin. Possible functions of the carbohydrate component of rhodopsin in the photoreceptor membrane are postulated.
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PMID:[Carbohydrate composition of wall-eyed pollock rhodopsin]. 724 56

CD59 is an 18-kDa glycoprotein widely expressed on human cells. An important structural feature of CD59 is its attachment to the cell surface via a glycosyl-phosphatidylinositol (GPI) anchor. CD59, like many GPI-anchored proteins, has been found in urine, serum, and other body fluids. The structures of the GPI anchor and the asparagine-linked sugar chain of a soluble form of CD59 in urine, U-CD59, were determined. Purified U-CD59 released 1 mol of inositol per mole of protein by nitrous acid deamination, which cleaved between glucosamine and inositol present commonly in the GPI anchor. This indicates that a GPI anchor, which ended with inositol, is linked at the carboxy terminus of U-CD59. The peptide containing an asparagine-linked sugar chain and the peptide containing a glycan portion of the GPI anchor were isolated after trypsin digestion of U-CD59. The asparagine-linked sugar chains and the glycan portion of the GPI anchor were isolated from these peptides following hydrazinolysis or deamination and dephosphorylation, respectively. Their structures were analyzed by sequential exoglycosidase digestion and methylation analyses. The structures of the asparagine-linked sugar chains of U-CD59 were biantennary complex type, only 4.2% of which are monosialylated. The backbone structure of the GPI anchor was similar to that of Try-panosoma brucei variant surface glycoprotein, but showed significant variations in its side-chain moieties. This is the first detailed structural analysis of the human GPI anchor and the first detailed analysis of the carboxyl-terminal structure of the soluble-form GPI-anchored protein. The results indicate that the backbone structure of the GPI anchor is conserved from parasites to human and that at least a part of the soluble-form GPI-anchored protein has the structure produced by the action of glycan-phosphatidylinositol-specific phospholipase D.
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PMID:Structural study on the glycosyl-phosphatidylinositol anchor and the asparagine-linked sugar chain of a soluble form of CD59 in human urine. 751 86

The structure of lipid A from the lipopolysaccharide of Rhizobium leguminosarum bv. phaseoli (wild type strain CE3) was investigated by alkylation analysis, nuclear magnetic resonance spectroscopy, and electrospray and fast atom bombardment mass spectrometry of the de-O-acylated lipid A. The lipid A carbohydrate backbone was shown to be a trisaccharide containing galacturonic acid, glucosamine, and the unique sugar 2-amino-2-deoxygluconic acid, previously unreported in lipopolysaccharides. Nuclear magnetic resonance spectroscopy and ethylation analyses revealed that the galacturonic acid is alpha-1,4-linked to the glucosamine, while the amino aldonic acid residue, which may exist as the 1,5-lactone, is attached as an aglycone to the glucosamine and, thus, occupies the reducing end of the molecule. The resulting backbone is hydrophilic and analogous to the commonly observed bisphosphorylated glucosamine disaccharide from enteric bacterial lipopolysaccharides in that both the nonreducing and reducing ends carry negatively charged substituents. The fatty acids of the R. leguminosarum lipid A are attached both as O- and N-acyl substituents to glucosamine and 2-aminogluconate. All fatty acids are hydroxylated consisting of 3-hydroxymyristate (3-OH-C14.0), 3-hydroxypentadecanoate (3-OH-C15.0), 3-hydroxypalmitate (3-OH-C16.0), 3-hydroxystearate (3-OH-C18.0), and 27-hydroxyoctacosanoate (27-OH-C28.0) in the approximate mole ratio 3:0.2:1:0.6:1. Unlike lipid As from enteric bacteria, the R. leguminosarum lipid A lacks 3-acyloxyacyl substituents; however, the long chain 27-hydroxy fatty acid carries ester-linked beta-hydroxybutyrate at the 27-hydroxy position. Fast atom bombardment mass spectrometry of the de-O-acylated lipid A demonstrated the presence of 2 molecular species that differ by 28 mass units due to fatty acid heterogeneity at the two amide linkages. One species carries amide-linked 3-OH-C14.0 and 3-OH-C16.0; the second species carries 3-OH-C14.0 and 3-OH-C18.0. Each molecular species also exists as the aldonolactone, yielding molecular ions at ((M+H)+)-18. The heterogeneity in the amide-linked fatty acids further distinguishes the Rhizobium lipid A from enteric lipid As.
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PMID:Structure of lipid A component of Rhizobium leguminosarum bv. phaseoli lipopolysaccharide. Unique nonphosphorylated lipid A containing 2-amino-2-deoxygluconate, galacturonate, and glucosamine. 818 46


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