1H NMR Characterization of a Hen Ovalbumin Tyrosinamide N-Linked Oligosaccharide Library

Dasilva, M.L.C.; Stubbs, Hilary J.; Tamura, Toshiaki; Rice, Kevin G.

doi:10.1006/abbi.1995.1255

Cited by 67 publications

(55 citation statements)

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“…Amelogenin Binds to K5 and Ovalbumin, a Glycoprotein with Terminal GlcNAc-Recombinant amelogenin (rM179) binds to both K5 and ovalbumin, another glycoprotein containing two residues of N-linked GlcNAc and one residue of O-linked GlcNAc (25). The dosimetric interaction between K5 and amelogenin differs from that of ovalbumin and amelogenin.…”

Section: Discussionmentioning

confidence: 99%

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Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Ravindranath

Basilrose

Ravindranath

et al. 2003

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

“…The values were corrected for background (wells without antigen). Ovalbumin was used as a positive control because it contains two residues of terminal GlcNAc (25) and BSA as a negative control.…”

Section: Methodsmentioning

confidence: 99%

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Ravindranath

Basilrose

Ravindranath

et al. 2003

Journal of Biological Chemistry

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“…Probably, the amino and hydroxyl groups required for amelogenin-sugar interaction are not accessible when sialic acid is in a bound state. However, amelogenin is able to recognize chitobiose and chitotetraose, as well as ovalbumin, in which GlcNAc also occurs as a terminal sugar (33) suggesting that C-2 and C-3 of the bound-GlcNAc is accessible to amelogenin. In this respect, amelogenin resembles a GlcNAc-specific lectin from the ascidian Didemnum ternatanum (43).…”

Section: Discussionmentioning

confidence: 99%

“…, 3Ј-N-acetylneuraminyllactose, 6Ј-N-acetylneuraminyllactose, 6Ј-N-acetylneuraminyl-N-acetyllactosamine, N-acetyl-neuraminyllactoneotetrose, chitobiose, chitotetraose, and the glycoproteins, fetuin and submaxillary mucin, representing sialoglyoproteins and ovalbumin (a protein with terminal GlcNAc) (33). All free sugars were diluted (1/10 in TBS, pH 6.3) in Eppendorf tubes and were warmed to 30°C before use.…”

Section: Expression Isolation and Purification Of Recombinant Mousementioning

confidence: 99%

Tyrosyl Motif in Amelogenins BindsN-Acetyl-d-glucosamine

Ravindranath

Moradian‐Oldak

Fincham

1999

Journal of Biological Chemistry

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Ameloblasts secrete amelogenins on the pre-existing enamel matrix glycoproteins at the dentine-enamel junction. The hypothesis that amelogenins may interact with enamel matrix glycoproteins is tested by hemagglutination of purified, native (porcine) and recombinant murine amelogenins (rM179 and rM166) and hemagglutination inhibition with sugars. Amelogenin agglutination of murine erythrocytes was specifically inhibited by N-acetylglucosamine ( 14 C]GlcNAc did indeed bind to this "amelogenin tyrosyl motif peptide" but not when the tyrosyl residues were substituted with phenylalanine or when the third proline was replaced by threonine. Significantly, this latter modification mimics a point mutation identified in a case of human X-linked amelogenesis imperfecta. The amelogenin tyrosyl motif peptide sequence showed a similarity to the secondary GlcNAc-binding site of wheat germ agglutinin.

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“…Materials N-linked glycans were released in a large-scale preparation with hydrazine [50,51] from the well-characterized glycoproteins (Sigma Chemical Co. Ltd., Poole, Dorset, UK) ribonuclease B [52], porcine thyroglobulin [53,54], chicken ovalbumin (found to contain small amounts of other ovo-glycoproteins) [55,56], and bovine fetuin [57]. Neutral glycans were obtained from fetuin and thyroglobulin by heating the released glycans with 1 % acetic acid for 1 h at 70°C.…”

Section: Methodsmentioning

confidence: 99%

MALDI-MS/MS with Traveling Wave Ion Mobility for the Structural Analysis ofN-Linked Glycans

Harvey

Scarff

Crispin

et al. 2012

J. Am. Soc. Mass Spectrom.

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The preference for singly charged ion formation by MALDI makes it a better choice than electrospray ionization for profiling mixtures of N-glycans. For structural analysis, fragmentation of negative ions often yields more informative spectra than fragmentation of positive ones but such ions are more difficult to produce from neutral glycans under MALDI conditions. This work investigates conditions for the formation of both positive and negative ions by MALDI from N-linked glycans released from glycoproteins and their subsequent MS/MS and ion mobility behaviour. 2,4,6-Trihydroxyacetophenone (THAP) doped with ammonium nitrate was found to give optimal ion yields in negative ion mode. Ammonium chloride or phosphate also yielded prominent adducts but anionic carbohydrates such as sulfated N-glycans tended to ionize preferentially. Carbohydrates adducted with all three adducts (phosphate, chloride, and nitrate) produced good negative ion CID spectra but those adducted with iodide and sulfate did not yield fragment ions although they gave stronger signals. Fragmentation paralleled that seen following electrospray ionization providing superior spectra than could be obtained by PSD on MALDI-TOF instruments or with ion traps. In addition, ion mobility drift times of the adducted glycans and the ability of this technique to separate isomers also mirrored those obtained following ESI sample introduction. Ion mobility also allowed profiles to be obtained from samples whose MALDI spectra showed no evidence of such ions allowing the technique to be used in conditions where sample amounts were limiting. The method was applied to N-glycans released from the recombinant human immunodeficiency virus glycoprotein, gp120.

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1H NMR Characterization of a Hen Ovalbumin Tyrosinamide N-Linked Oligosaccharide Library

Cited by 67 publications

References 0 publications

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Tyrosyl Motif in Amelogenins BindsN-Acetyl-d-glucosamine

MALDI-MS/MS with Traveling Wave Ion Mobility for the Structural Analysis ofN-Linked Glycans

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