Determination of amino sugars and amino acids in glycoconjugates using precolumn derivatization with o-phthalaldehyde

Altmann, Friedrich

doi:10.1016/0003-2697(92)90164-3

Cited by 90 publications

(51 citation statements)

References 15 publications

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“…From the same Amb a 4 preparation, amino acids were determined by HPLC of o-phthalaldehyde derivatives (16). This allowed a correlation of sugar and protein content.…”

Section: Methodsmentioning

confidence: 99%

“…Other Analytical Techniques-Amino acids were determined using either o-phthaldehyde and 2-mercaptoethanol for primary amino acids or o-phthaldehyde, 3-mercaptopropionic acid and 9-fluorenylmethyl-chloroformate for second-ary amino acids as described (16). To obtain N-terminal sequence information purified natural Amb a 4 was separated by SDS-PAGE and electroblotted onto polyvinyl difluoride membranes (Millipore, Bedford, MA).…”

Section: Methodsmentioning

confidence: 99%

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A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Léonard

Wopfner

Pabst

et al. 2010

Journal of Biological Chemistry

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Art v 1, the major pollen allergen of the composite plant mugwort (Artemisia vulgaris) has been identified recently as a thionin-like protein with a bulky arabinogalactan-protein moiety. A close relative of mugwort, ragweed (Ambrosia artemisiifolia) is an important allergen source in North America, and, since 1990, ragweed has become a growing health concern in Europe as well. Weed pollen-sensitized patients demonstrated IgE reactivity to a ragweed pollen protein of apparently 29 -31 kDa. This reaction could be inhibited by the mugwort allergen Art v 1. The purified ragweed pollen protein consisted of a 57-amino acidlong defensin-like domain with high homology to Art v 1 and a C-terminal proline-rich domain. This part contained hydroxyproline-linked arabinogalactan chains with one galactose and 5 to 20 and more ␣-arabinofuranosyl residues with some ␤-arabinoses in terminal positions as revealed by high field NMR. The ragweed protein contained only small amounts of the single hydroxyproline-linked ␤-arabinosyl residues, which form an important IgE binding determinant in Art v 1. cDNA clones for this protein were obtained from ragweed flowers. Immunological characterization revealed that the recombinant ragweed protein reacted with >30% of the weed pollen allergic patients. Therefore, this protein from ragweed pollen constitutes a novel important ragweed allergen and has been designated Amb a 4.The pollen of common ragweed (Ambrosia artemisiifolia) is a major cause of hay fever and associated asthma in Northern America. During the past few decades, ragweed has started to spread in many parts of central Europe, where it has become a serious health problem in the sensitized population. Several initiatives have formed to prevent further spread in e.g. France, Austria or southern Germany. The Compositae (or Asteraceae) family is one of the largest families of flowering plants, but only a few are important allergenic sources. These include Ambrosia (ragweed), Artemisia (mugwort), Helianthus (sunflower), and Parthenium (feverfew). It was further demonstrated that sera of mugwort allergic patients show considerable cross-reactivity with ragweed pollen extracts (1, 2). IgE-binding to mugwort allergens in immunoblots was inhibited effectively by ragweed pollen extract (1), which indicates close homology of the essential allergens in ragweed and mugwort pollen. So far, six groups of allergens have been identified in ragweed pollen. Most patients were classified as ragweed allergic if they reacted with the pectate lyases of the Amb a 1/2 group (3, 4). The homologous pectate lyase Art v 6 in mugwort has been reported to play only a minor role in allergic disease. Amb a 6 (lipid transfer protein), Amb a 8 (profilin), Amb a 9 and Amb a 10 (both calcium-binding proteins) are small proteins belonging to the group of well known cross-reactive pan-allergens (1, 4 -8). Amb a 7 and the fragment Amb a 3 are plastocyanins and are described only as minor ragweed allergens (9).In mugwort pollen, the major allergen is Art v 1, a protein w...

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“…From the same Amb a 4 preparation, amino acids were determined by HPLC of o-phthalaldehyde derivatives (16). This allowed a correlation of sugar and protein content.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Léonard

Wopfner

Pabst

et al. 2010

Journal of Biological Chemistry

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“…Lyophilized Nglycans were dissolved in water and subject to either MALDI-TOF analysis (see below) or pyridylamination (17,20,21). The final yield of N-glycans was estimated as being 10 -15 nmol, as judged by determination of the amino sugar content (22) and assuming two GlcNAc residues/N-glycan.…”

Section: Methodsmentioning

confidence: 99%

“…28 in order to generate GnGnF 6 ). The exact concentration of acceptor substrate was determined by analysis of the GlcNAc and amino acid content (22).…”

Section: Methodsmentioning

confidence: 99%

Identification of Core α1,3-Fucosylated Glycans and Cloning of the Requisite Fucosyltransferase cDNA from Drosophila melanogaster

Fabini

Freilinger

Altmann

et al. 2001

Journal of Biological Chemistry

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152

179

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For many years, polyclonal antibodies raised against the plant glycoprotein horseradish peroxidase have been used to specifically stain the neural and male reproductive tissue of Drosophila melanogaster. This epitope is considered to be of carbohydrate origin, but no glycan structure from Drosophila has yet been isolated that could account for this cross-reactivity. Here we report that N-glycan core ␣1,3-linked fucose is, as judged by preabsorption experiments, indispensable for recognition of Drosophila embryonic nervous system by anti-horseradish peroxidase antibody. Further, we describe the identification by matrix-assisted laser desorption-ionization time-of-flight mass spectrometry and high performance liquid chromatography of two Drosophila N-glycans that, as already detected in other insects, carry both ␣1,3-and ␣1,6-linked fucose residues on the proximal core GlcNAc. Moreover, we have isolated three cDNAs encoding ␣1,3-fucosyltransferase homologues from Drosophila. One of the cDNAs, when transformed into Pichia pastoris, was found to direct expression of core ␣1,3-fucosyltransferase activity. This recombinant enzyme preferred as substrate a biantennary core ␣1,6-fucosylated N-glycan carrying two non-reducing N-acetylglucosamine residues (GnGnF 6 ; K m 11 M) over the same structure lacking a core fucose residue (GnGn; K m 46 M). The Drosophila core ␣1,3-fucosyltransferase enzyme was also shown to be able to fucosylate N-glycan structures of human transferrin in vitro, this modification correlating with the acquisition of binding to anti-horseradish peroxidase antibody.Glycoproteins from plants and invertebrates are often highly immunogenic and many antibodies (both IgG and IgE) directed against them bind to core ␣1,3-fucose and/or ␤1,2-xylose residues of their N-linked oligosaccharides (1-7); since these modifications are present across plant species and one or the other modification is present in a number of invertebrates, these antibodies are highly cross-reactive. Indeed, polyclonal antibodies to horseradish peroxidase (anti-HRP) 1 have been used for nearly two decades to specifically stain neurons, and their growth pathways, in Drosophila melanogaster (8 -11); similar staining has also been described in grasshopper (11), whereas in Caenorhabditis elegans 10% of neurons are stained by this antibody (12). A number of proteins in Drosophila, such as an Na ϩ ,K ϩ ATPase christened Nervana, a receptor tyrosine phosphatase, and cell adhesion molecules (e.g. fasciclin I and II, neurotactin and neuroglian), have been found to bind anti-HRP (9 -11, 13, 14); however, no data on their glycosylation have been described. A number of Drosophila nac (neurally altered carbohydrate) mutants have been described, which are defective in anti-HRP staining of adult flies and display wing morphological defects (15) and, when under cold stress, some minor behavioral and eye developmental abnormalities (9). Neither the affected gene(s) nor the underlying biochemical defect(s) have been identified.As compared with the amount o...

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“…Separation of amino acids was done using a einerhyperphil ODS 250 x 4 mm-column after pre-column derivatisation with OPA (orthophtalaldehyde) (ALVA, 1983 andAltmann, 1992). Amino acid compositions for the soybean meal and Guar Korma meal feed ingredients are shown in Table 3.…”

Section: Essential Amino Acids Composition Of Soybean Meal and Guar Kmentioning

confidence: 99%

Impact of replacement of soybean meal with guar korma meal on growth performance and some physiological parameters of the Nile Tilapia (Oreochromis niloticus) fingerlings.

S¹,

El-Zayat²,

Abdel³

et al. 2016

Egypt. J. of Aquatic Biolo. and Fish.

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This study aimed to evaluate the partial and complete substitution of soybean meal as crude protein by various levels (0%, 25%, 5٠% , 75% and 100%) of guar korma meal (GKM) (Cyamopsis tetragonolobus) in the Tilapia diet on growth performance, feed utilization, carcass composition and physiological parameters (ALT, AST and glucose level). Water quality parameters were checked and evaluated on a daily basis and the other factors were analyzed fortnightly of the Nile Tilapia (Oreochromis niloticus) fingerlings. Five isonitrogenous (30% crude protein) and isocaloric (4300 kcal/kg gross energy) diets were formulated to contain guar korma meal at 0 , 9.5 , 18.5, 27.75 and 37 % crude protein levels by replacing soybean meal at 0 , 25, 50, 75 and 100% crude protein, respectively. An experimental diet containing 37 % soybean meal and 0% guar meal protein was used as a control diet. All fish were fed at 5 % body weight / day in three replicates. Results of the present study concluded that guar korma meal is a promising ingredient source of protein in aqua feeds and can be included up to 18.5 % crude protein by replacing 50% of soybean meal crude protein during feed formulation for the Nile Tilapia (O. niloticus) diets system without affecting the growth performance and feed utilization.

show abstract

Determination of amino sugars and amino acids in glycoconjugates using precolumn derivatization with o-phthalaldehyde

Cited by 90 publications

References 15 publications

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Identification of Core α1,3-Fucosylated Glycans and Cloning of the Requisite Fucosyltransferase cDNA from Drosophila melanogaster

Impact of replacement of soybean meal with guar korma meal on growth performance and some physiological parameters of the Nile Tilapia (Oreochromis niloticus) fingerlings.

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