Structure of N-glycans on the S3- and S6- stylar self-incompatibility ribonucleases of Nicotiana alata

Oxley, D., Munro, S. L. A., Craik, D. J. and Bacic, A. (1996) Structure of N-glycans on the S3- and S6- stylar self-incompatibility ribonucleases of Nicotiana alata. Glycobiology, 6 6: 611-618. doi:10.1093/glycob/6.6.611


Author Oxley, D.
Munro, S. L. A.
Craik, D. J.
Bacic, A.
Title Structure of N-glycans on the S3- and S6- stylar self-incompatibility ribonucleases of Nicotiana alata
Formatted title
Structure of N-glycans on the S3- and S6- stylar self-incompatibility ribonucleases of Nicotiana alata
Journal name Glycobiology   Check publisher's open access policy
ISSN 0959-6658
1460-2423
Publication date 1996-09
Sub-type Article (original research)
DOI 10.1093/glycob/6.6.611
Volume 6
Issue 6
Start page 611
End page 618
Total pages 8
Place of publication Cary, NC, United States
Publisher Oxford University Press
Language eng
Formatted abstract
Self-incompatibility is a mechanism developed by many plants to prevent inbreeding. The products of the selfincompatibility (S)-locus in the styles of solanaceous plants are a series of glycoproteins with ribonuclease activity. In this study, we report on the N-glycans from the stylar selfincompatibility S3- and S6-ribonucleases of Nicotiana alata, which were enzymically released and fractionated by high-pH anion-exchange HPLC. A total of 14 N-glycans were identified and characterized by a combination of electrospray-ionization mass-spectrometry, 1H-NMR spectroscopy, chemical degradation, and methylation analyses. This pattern of N-glycosylation is much more complex than that previously found on the N.alata S1- and S2-RNases each of which contained only four N-glycans.
Keyword N-glycan
Nicotiana alata
ribonuclease
self-incompatibility
Carbohydrate Moiety
Sugar Chains
S-Proteins
Glycoprotein
Spectroscopy
Oligosaccharides
Sequence
Pollen
Expression
Cloning
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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