Purification and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Petunia hybrida
- 1 January 1990
- journal article
- research article
- Published by Springer Nature in Plant Molecular Biology
- Vol. 14 (1), 93-102
- https://doi.org/10.1007/bf00015658
Abstract
We report isolation and N-terminal amino acid sequencing of three style glycoproteins, which segregate with three S (self-incompatibility) alleles of Petunia hybrida. The S-glycoproteins were expressed mainly in the upper part of the pistil and showed an increasing concentration during flower development. The glycoproteins were purified by a combination of ConA-Sepharose and cation exchange fast protein liquid chromatography. The amount of S-glycoproteins recovered from style extracts varied from 0.5 to 1.6 μg per style, which was 40–60% of the amount recovered by a simplified analytical method. N-terminal amino acid sequences of S1-, S2- and S3-glycoprotein showed homology within the fifteen amino terminal residues. These amino acid sequences were compared with the previously published sequences of S-glycoproteins from Nicotiana alata and Lycopersicon peruvianum.Keywords
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