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N-Linked Glycan Chains on S-Allele-Associated Glycoproteins from Nicotiana alata.
Author(s) -
James R. Woodward,
Antony Bacic,
Willi JahnenDechent,
Adrienne E. Clarke
Publication year - 1989
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.1.5.511
Subject(s) - glycoprotein , glycan , locus (genetics) , allele , biochemistry , cleavage (geology) , membrane glycoproteins , biology , chemistry , gene , genetics , fracture (geology) , paleontology
The products of the self-incompatibility locus of flowering plants are glycoproteins. The specificity of different alleles at this locus might be expressed through differences in either amino acid sequences or by the glycan substituents. We have investigated the numbers of N-linked glycan chains on the S-glycoproteins and obtained information on their structure by enzymic cleavage with N-glycanase and endo-[beta]-N-acetylglucosaminidase H. In addition to there being variation in the numbers of chains on the S-glycoproteins, each glycoprotein appears to consist of a spectrum of "glycoforms" bearing chains of differing type and fine structure. This microheterogeneity in N-linked glycan chains may be functionally significant.

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