Stimson, E and Hope, J and Chong, A and Burlingame, AL (1999) Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry , 38 (15) 4885 - 4895.
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The murine prion protein PrP gene encodes a protein of 254 amino acids with two consensus sites for Asn-linked glycosylation at codons 180 and 196. A partial site-specific study of the N-linked glycans from hamster PrP has previously been carried out by mass spectrometry [Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Biochemistry 32, 1991-2002] and revealed that the glycosylation at Asn-181 (equivalent to mouse 180) is heterogeneous, comprising over 30 glycoforms. The identification of the glycosylated peptide spanning Asn-197 was not reported. Recent technical advances in electrospray mass spectrometry now provide the sensitivity to detect low femtomole quantities of glycopeptides with >5000 mass resolution and 30 ppm mass measurement [Medzihradszky, K. F., Besman, M. J., and Burlingame, A. L. (1998) Rapid Commun. Mass Spectrom. 12, 472-478]. This performance coupled with stepwise exoglycosidase digestion has been employed to establish the differential nature of the structural complexity (glycoforms) of the glycans at Asn-180 and Asn-196 from a single strain infected with the ME7 strain. Some sixty structures have been found characterized by neutral and sialylated bi-, tri-, and tetraantennary complex-type bearing outer-arm alpha(1-3)-fucosylation (the Lewisx and sialyl-Lewisx epitopes), core alpha(1,6) fucosylation, and the presence of terminal HexNAc residues. The Lewisx trisaccharide is the major nonreducing structure at Asn-180, and significant amounts of both Lewisx and sialyl Lewisx epitopes are observed at Asn-196. The abundance of the Lewisx and sialyl Lewisx epitopes on murine PrPSc may indicate a role for these structures in the normal function of PrPC or the pathophysiology of PrPSc
|Title:||Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions|
|Additional information:||UI - 99218099 LA - Eng RN - EC 3.2.1. (Glycoside Hydrolases) RN -0 (Polysaccharides) RN - 0 (Prions) RN - 7006-34-0 (Asparagine) PT - JOURNAL ARTICLE ID - RR 01614/RR/NCRR DA - 19990517 IS -0006-2960 SB - M CY - UNITED STATES JC - A0G AA - Author EM -199907|
|Keywords:||Prions, Proteins, Asparagine, Id, United States, Acids, amino acid, Amino Acid Sequence, Amino Acids, Animal, Biochemistry, cancer, Carbohydrate Conformation, Carbohydrate Sequence, chemistry, Chromatography, High Pressure Liquid, Epitopes, GENE, Glycopeptides, Glycoside Hydrolases, Glycosylation, Hydrolysis, metabolism, Mice, Molecular Sequence Data, Polysaccharides, Spectrum Analysis, Mass, Support, U.S.Gov't, P.H.S., hamster, S, mouse, peptides, Nature, Structure, function, pathophysiology|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
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