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At least 1,333 records · Page 74Linked to original sources
PubMed1978

Studies on the question of conventional immunoglobulin on thymocytes from primitive vertebrates. I. Presence of anti-carbohydrate antibodies in rabbit anti-trout Ig sera.

An unexpected cross-reactivity between trout immunoglobulin (Ig) and keyhole limpet hemocyanin (KLH) was observed. Rabbit antisera to KLH were capable of binding to radioiodinated trout Ig and, conversely, antitrout Ig reacted with KLH. The cross-reactive antibodies were not found in preimmune sera and did not arise because of a common contaminant in the two immunizing preparations. The molecular basis of the cross-reactivity was found to reside in the carbohydrate moieties. Isolated glycopeptides from KLH and trout Ig were efficient inhibitors of the cross-reactivity. Furthermore, L-fucose was capable of inhibiting the cross-reactivity, whereas other monosaccharides tested did not. Absorption of anti-KLH with trout Ig and anti-trout Ig with KLH effectively removed the cross-reactive antibodies and only slightly affected the titer to their respective homologous antigens. Antibodies with specificity for L-fucose were isolated from anti-KLH and anti-trout Ig sera by passage over affinity columns and elution with the monosaccharide.

Absorption↗
PubMed1988

[The saccharide components of wood hydrolysates--a constituent part of the fermentation media for the biosynthesis of beta-lactam antibiotics].

Spruce and ash wood were subjected to acid hydrolysis. The hydrolysates were paper chromatographed for the presence of saccharides. The following monosaccharides were detected: D-xylose, D-mannose, D-glucose, D-galactose and L-arabinose. The monosaccharides and L-rhamnose in addition in the form of concentrated solutions were used as part of lactose in production of penicillin V. Similarly, the whole amounts of D-glucose and saccharose were substituted in biosynthesis of cephalosporin C. With regard to the results it follows that hydrolysates of the conifers and especially of the hardwood can substitute part of the fermentation medium components in production of penicillin V and cephalosporin C.

Acremonium↗
PubMed1986

Simple sugars with affinity for the macrophage asialoglycoprotein receptor are adjuvants for the humoral immune response to neuraminidase-treated sheep erythrocytes.

The influence of monosaccharides on the humoral immune response of mice to normal and neuraminidase-treated sheep red blood cells (SRBC) was investigated. In these studies, both the sugars and antigen were administered i.p. D-Galactose displayed adjuvant activity for neuraminidase-treated but not for normal SRBC. This activity was optimal at an antigen dose of 3 X 10(6) cells. Other monosaccharides with an axial hydroxyl group at position 4 and D-mannose-6-phosphate behaved like D-galactose, whereas structurally unrelated sugars did not. The adjuvant activity of the saccharides corresponded to the affinity of the substances for the asialo-glycoprotein receptor. The adjuvant effects were also expressed in cobra venom factor-treated and C5-deficient mice. This suggests that blockade of the asialo-receptor rather than complement is involved in this form of immunoadjuvant activity. The findings are also in support of our hypothesis that obstruction of nonimmune antigen elimination, in this case at the level of macrophages, would be one of the mechanisms underlying immunologic adjuvant activity.

Adjuvants, Immunologic↗
PubMed1979

Radioassays of blood group M, N and T (Thomsen-Friedenreich) antigens.

Radioassays employing the double-antibody or Farr techniques were developed for the M, N and T antigens. Blood group glycoproteins were isolated by butanol extraction of red cell stroma and iodinated by the chloramine-T technique. The final purity of glycoprotein was over 75% as judged by radioimmunoassay (RIA). T activation of glycoprotein was obtained with neuraminidase. A specific RIA was obtained for the M antigen and was sensitive to approximately 10 ng of glycoprotein or glycopeptide. In the RIA system rabbit anti-M displayed a higher affinity for M glycoprotein than for M glycopeptide. A RIA that was entirely specific for the N antigen, could not be obtained. A radioassay, obtained for the T antigen with peanut agglutinin in the Farr technique, was sensitive to approximately 100 ng of T antigen and was readily inhibitable by monosaccharides. A RIA, obtained for the T antigen with rabbit anti-T, was entirely specific and sensitive to approximately 1 ng of T activated glycoprotein or glycopeptide but was not inhibitable by monosaccharides.

Blood Group Antigens↗
PubMed1982

Stimulation of mannose-binding activity in the rabbit alveolar macrophage by simple sugars.

Mammalian alveolar macrophages are known to bind glycoconjugates with terminal D-mannosyl residues (Stahl, P. D., Rodman, J. S. Miller, M. J., and Schlesinger, R. H. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 1399-1403). Although macromolecules containing D-mannosyl residues, such as bovine serum albumin modified with 2-imino-2-methoxyethyl 1-thio-alpha-D-mannopyranoside (mannose-BSA) (Lee, Y. C., Stowell, C. P., and Krantz, M. J. (1976) Biochemistry 15, 3956-3963), were very potent inhibitors of 125I-mannose-BSA binding to macrophages, the monosaccharides D-mannose, L-fucose, N-acetyl-D-glucosamine, and D-glucose doubled to tripled the binding of 125I-mannose-BSA to intact rabbit lung macrophages at 2 degrees C. The monosaccharide concentration required for maximum stimulation and the extent of stimulation were dependent on the number of D-mannosyl residues attached to the BSA ligand. The lower the number of D-mannosyl residues coupled to BSA, the smaller the effect by D-mannose and the lower the D-mannose concentration at which it occurred. Equilibrium binding analysis indicated that the apparent affinity of cell surface receptor for ligand increased from Kd = 1.0 nM to Kd = 0.3 nM under conditions of maximal stimulation of 125I-mannose43-BSA binding.

Animals↗
PubMed1980

Penetration of chick embryo erythrocytes by toxoplasma gondii tachyzoites in simplified incubation media.

The ability of Toxoplasma gondii tachyzoites to penetrate chick embryo erythrocytes (CEE) and the extent of penetration were examined in various simplified, incubation media. Toxoplasma gondii penetrated CEE well in serum-free Eagle's minimum essential medium or in Hanks' balanced salt solution, but much less in phosphate buffered saline (PBS). However, the addition of glucose alone to PBS substantially increased the penetration. A similar effect was seen with other monosaccharides, except galactose. A further, marked increase in penetration was noticed if magnesium ion (but not calcium ion) was added to PBS containing glucose. The present results indicate that T. gondii can penetrate CEE well in simplified incubation solutions such as PBS only when magnesium ion and a monosaccharide are added. Their possible role is discussed in relation to cellular adhesiveness, because the adherence of the parasite to the host cell membrane may be the first step in the penetration process.

Animals↗
PubMed1982

A new complement-dependent bactericidal factor found in nonimmune mouse sera: specific binding to polysaccharide of Ra chemotype Salmonella.

It has been shown that nonimmune mouse sera contain a complement-dependent bactericidal factor that reacts specifically with Ra chemotype Salmonella. In this study we investigate a specific determinant to which this factor binds. This factor bound to Ra chemotype lipopolysaccharide (LPS) but not to S or Re chemotype LPS. The binding was markedly inhibited by N-acetyl-D-glucosamine (GlcNAc), which was the nonreducing terminal of the Ra polysaccharide chain and by certain monosaccharides structurally relating to L-glycero-D-mannoheptose, a terminal component of a side branch of Ra polysaccharide. The factor bound to the Ra bacteria could be eluted with a medium containing GlcNAc. These results indicate that the specific determinant is the polysaccharide region of LPS characteristic of Ra chemotype Salmonella. Ca2+ but not Mg2+ was required for the specific binding of the factor to cells of Ra bacteria. A molecule composed of a polypeptide of 28,000 m.w. was found in the active fraction obtained by the monosaccharide elution. However, no polypeptides corresponding to light and heavy chains of mouse immunoglobins were detected from the active fraction.

Acetylglucosamine↗
PubMed1978

[Characteristics of the polysaccharide-containing somatic antigens isolated from the K-1 strain of the plague microbe and its antibiotic-resistant variants].

Immunochemical analysis of 2 polysaccharide-containing structures of the lypopolysaccharide of the plague causative agent (main somatic antigen and lipopolysaccharide) isolated from K-1 strain and a number of its antibiotic resistant mutants was carried out. It was shown that development of resistance to streptomycin alone or its combination with monomycin did not cause detectable changes in the monosaccharide composition and serological properties of the cultures tested. More significant changes associated with development of complex resistance, i.e. K-1 (Strr leads to Penr leads to Tetr) were accompanied by a decrease in the content of hexozamine and serological activity of the main somatic antigen determining the O-specificity of the lipopolysaccharide. Defective changes in the monosaccharide composition and serological properties of both the main somatic antigen and the polysaccharide were observed in the yellow variant of the streptomycin resistant mutant K-1.

Anti-Bacterial Agents↗
PubMed1982

Cytochalasin B. A natural photoaffinity ligand for labeling the human erythrocyte glucose transporter.

[3H]Cytochalasin B was found to be a natural photoaffinity ligand which at low concentrations could be photoincorporated into specific proteins of the human erythrocyte plasma membrane associated with high affinity binding sites of this molecule. In the presence of L-glucose, the polypeptide region referred to as zone 4.5 on sodium dodecyl sulfate-polyacrylamide gel electrophoretograms was photolabeled with [3H]cytochalasin B. At least two major peaks could be resolved in this region, one at approximately 50,000 daltons and the other at approximately 47,000 daltons. In addition, this incorporation was partially blocked when D-glucose was substituted for L-glucose in these experiments. Incorporation was time-dependent upon photolysis, did not occur in the absence of light, and was not reversible under the harsh conditions of gel electrophoresis. This suggests a covalent incorporation of this ligand into polypeptides previously identified as being associated with monosaccharide transport in these cells. In addition, soluble G-actin from muscle was labeled, but at a level 100-fold lower than transporter polypeptides. These experiments suggest that this technique may prove useful in identifying monosaccharide transporter proteins in other cell systems as well as other types of cellular proteins associated with high affinity cytochalasin binding.

Affinity Labels↗
PubMed1994

Molecular biology of sugar transporters of the plant plasma membrane.

Plants possess highly efficient transport systems for organic substances such as monosaccharides and disaccharides. In many lower plants these transport systems can be used for heterotrophic growth in the absence of light. In higher plants which are a complex mosaic of autotrophic and heterotrophic cells, tissues and organs, they play an important role in the distribution of assimilated carbon amongst these various parts. Genes and cDNAs encoding transport proteins for mono-or disaccharides have been cloned recently. The relationship of these transporters to a large superfamily of uni-, sym-, and antiporters cloned from many other organisms is discussed. The paper describes strategies for cloning, heterologous expression (in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Xenopus oocytes and heterologous plant systems), and functional characterization of individual transporters. Data on the tissue-specific expression of two monosaccharide transporters from Arabidopsis thaliana will be presented and possible glycosylation of the proteins is discussed.

Biological Transport↗
PubMed1994

Rat natural killer cell antigen, NKR-P1, related to C-type animal lectins is a carbohydrate-binding protein.

Natural killer receptor protein 1 (NKR-P1, a family of proteins), which is a dimeric transmembrane protein predominantly on rat and murine natural killer cells, contains an extracellular motif related to calcium-dependent animal lectins. The domain architecture of this protein and the finding that its cross-linking with antibody results in activation of natural killer cells make it a promising candidate for a receptor function. We have expressed a full-length NKR-P1 protein of the rat in COS cells and prepared soluble extracellular fragments by controlled proteolysis or by expression of truncated cDNA in bacteria. Dimerization of soluble NKR-P1 is predominantly dependent on the presence of an intact juxta-membrane stalk region and independent of N-glycosylation. Binding and inhibition studies using monosaccharides and neoglycoconjugates indicate that NKR-P1 is a lectin with a preference order of GalNAc > GlcNAc >> Fuc >> Gal > Man. At neutral pH, Ca2+ is tightly associated with the protein such that only a proportion can be removed by 10 mM EGTA. However, NKR-P1 can be decalcified completely at pH 10 with a total loss of carbohydrate binding. After recalcification at pH 8, carbohydrate binding is completely restored. Thus, NKR-P1 differs from other calcium-dependent animal lectins investigated so far in its pattern of monosaccharide recognition and in the tightness of Ca2+ binding.

Animals↗
PubMed1993

Changes in carbohydrate composition in human milk over 4 months of lactation.

This study aimed to examine the carbohydrate content (monosaccharides, lactose, and oligosaccharides) of human milk over 4 months of lactation to determine whether any changes occurred over time. Milk samples from 46 mothers, who delivered at term, were collected at 4th, 10th, 30th, 60th, 90th, and 120th days after delivery. Carbohydrates were measured by high-pressure liquid chromatography. Mean lactose concentration (+/- SD) increased from 56 +/- 6.06 g/L on day 4 to 68.9 +/- 8.16 g/L on day 120. Oligosaccharide level decreased from 20.9 +/- 4.81 g/L to 12.9 +/- 3.30 g/L, respectively. Monosaccharides represented only 1.2% of total carbohydrates. The changes in carbohydrate composition found indicate that carbohydrate synthesis by the mammary gland is a dynamic process. The physiological and biological relevance of human milk oligosaccharides is also discussed.

Carbohydrates↗
PubMed1996

Triglycerides, fatty acids, sterols, mono- and disaccharides and sugar alcohols in human milk and current types of infant formula milk.

OBJECTIVE: To investigate differences in the fatty acid composition, sterols, minor carbohydrates and sugar alcohols between human and formula milk. DESIGN: We analyzed the concentrations of triglycerides, sterols, di- and monosaccharides and sugar alcohols, as well as the fatty acid composition of 10 currently available types of formula milk for term babies. Results were compared with mature human milk from 99 exclusively breast-feeding Dutch women, who collected 24-hour samples in the second week (n = 99), sixth week (n = 99) and 3 months (n = 25) after delivery. Infant formula milk data were considered different if they fell outside the mean +/- 2s.d. range of corresponding human milk data. RESULTS: The triglyceride concentrations in human milk were lower than those of the formula milk, possibly due to an incomplete collection of fat-rich hindmilk. Formula milks tended towards a higher proportion of medium chain fatty acids and lower proportions of longer-chain polyunsaturated fatty acids. Formulas had cholesterol concentrations 3-35 times lower, and much higher phytosterol concentrations, compared with the human milk. In the formula milk types the glucose, sorbitol and myoinositol concentrations were generally lower, whereas the fucose and erythreitol concentrations were in the lower mean +/- 2s.d. human milk range. The galactose concentrations in the formulas were generally higher. CONCLUSIONS: Formula milk and human milk differ considerably in fatty acid composition and concentrations of cholesterol, phytosterols, monosaccharides and sugar alcohols. The biological consequences of these differences in composition are uncertain.

Carbohydrates↗
PubMed1996

Sulphated mucin oligosaccharides from porcine small intestine analysed by four-sector tandem mass spectrometry.

The fraction of sulphated oligosaccharide alditols isolated from mucin glycopeptides of porcine small intestine 'insoluble' mucin complex was analysed by negative-ion fast atom bombardment (FAB) tandem mass spectrometry. Collision-induced dissociation (CID) tandem mass spectra of native and peracetylated species were compared with standards of sulphated monosaccharides. The tandem mass spectra revealed structural information of the carbohydrate sequence and sulphate position. Negative-ion FAB ionization of the peracetylated sulphated oligo-saccharide alditols was at least three times more sensitive than that of the native sulphated oligosaccharide alditols, as revealed by comparing the signal-to-noise ratios, and allowed the detection of eleven compared with six pseudo-molecular ions. Fourteen structures were determined from the CID tandem mass spectra obtained. The main sulphation site was C-6 of an N-acetylglucosamine 6-linked to the N-acetylgalactosaminitol. C-3 of the N-acetylgalactosaminitol could be unsubstituted or extended with a series of up to three monosaccharide residues including blood group H determinants and blood group A determinants. Also, the sulphated N-acetylglucosamine could be further extended. The most abundant structure was a monosulphated trisaccharide with the sequence Gal-->3(SO3-->6GlcNAc-->6)GalNAcol. The sulphation at C-6 of N-acetylglucosamine seems to be a common feature for O-linked oligosaccharides, and has been described both for skeletal keratan sulphates and respiratory mucin oligosaccharides. Low-abundance ions were also detected from oligosaccharides with sulphation at C-3 of an amino sugar residue. This seems to be a novel sulphation site for mucin oligosaccharides.

Acetylation↗
PubMed2000

Mass spectrometry of partially methylated alditol acetates derived from hydroxyethyl starch.

The degradation and derivatization of hydroxyethyl starch to partially methylated alditol acetates (PMAAs) allows its detection by gas chromatography/mass spectrometry. The derivatization was performed by permethylation of the carbohydrate, hydrolysis of the permethylated polysaccharide, reduction of the resulting monosaccharides to alditoles and finally acetylation. A close similarity in the fragmentation of the PMAAs obtained was observed in both electron ionization (EI) and chemical ionization (CI) mass spectra owing to the comparable structures of the derivatives. CI measurements permitted the recognition of introduced hydroxyethyl groups in the glucose residues by detection of [M(+)+1]-60 signals. Investigations concerning the EI fragmentation schemes allowed secure determinations of monohydroxyethyl monosaccharides and differentiations between the possible positions (C-2, C-3 and C-6) of the substituted hydroxyethyl groups. Proposed generations of the main fragment ions are presented.

Gas Chromatography-Mass Spectrometry↗
PubMed1997

Immunoreactivities of polyclonal and monoclonal anti-T and anti-Tn antibodies with human carcinoma cells, grown in vitro and in a xenograft model.

Human polyclonal, monospecific anti-T and -Tn antibodies were found to be reactive in ELISA tests with human ovarian (IGROV-1, OVCAR-3 and SKOV-3), breast (SKBr-3 and T47D)- and oral (KB)-carcinoma cell lines, but less so or non-reactive with normal epithelia and fibroblasts. The direct binding radioimmunoassay, using 125I-labeled human antibodies, to the IGROV-1 cancer cells was inhibited by homologous unlabeled antibodies of the same concentration, but not by the respective immunodominant haptenic monosaccharides (Gal for T and GalNAc for Tn). Rodent ascitic monoclonal anti-T (Ca3114 and Ca3741) and anti-Tn (Ca3250, Ca3268 and Ca3638) antibodies were also reactive with the ovarian- and breast-cancer cells, as measured by FACS and ELISA tests, but to a lower extent than the polyclonal human antibodies. Both the monoclonal anti-T (Ca3741) and anti-Tn (Ca3250 and Ca3638) antibody-binding reactivities were significantly inhibited by the haptenic free monosaccharides. Addition of the above MAbs to IGROV-1 ovarian-cancer or T47D breast-cancer cells cultured in vitro resulted in significant cytological change and inhibition of the viability of the tumor cells, but not of normal epithelial breast cells. This effect on viability was shown to be complement-independent, yet it was profoundly influenced by the concentration of the serum added to the assay medium. In vivo biodistribution of the anti-T (Ca3114) and anti-Tn (Ca3638) MAbs administered i.p. to athymic IGROV-1 tumor-bearing CD1 female nude mice revealed higher 125I-labeled antibody accumulation in the tumor xenografts and in their lung tissues, as compared with other organs of the same mice tested. The above results thus suggest the feasibility of utilizing these antibodies in immunotherapy and drug targeting.

Animals↗
PubMed2000

Lyophilization of cationic lipid-protamine-DNA (LPD) complexes.

Cationic lipid-based gene delivery systems have shown promise in transfecting cells both in vitro and in vivo. However, these systems tend to form aggregates in liquid formulation during storage, which has limited their clinical applications. As a result, lyophilization of these systems has recently become a subject of increasing interest. In this paper, lyophilization of LPD, a novel cationic lipid-based gene delivery system, was studied. Both particle size and transfection efficiency could be preserved in the presence of sufficient amount of appropriate lyoprotectant. A series of monosaccharides and disaccharides, including dextrose, galactose, mannose, lactose, maltose, sucrose and trehalose, were evaluated for their lyoprotective effect and disaccharides showed more superior protection to monosaccharides. The effect of different freezing protocols for lyophilization was also evaluated and no significant difference was found. However, for freeze-thawing, fast freezing caused less aggregation. Finally, nonlyophilized LPD and LPD lyophilized with 10% sucrose were stored at different temperatures and their stability was followed for eight weeks. Lyophilized LPD could be stored at room temperature without significant change in particle size or loss of transfection efficiency.

Animals↗