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Purification and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Petunia hybrida

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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.

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Broothaerts, W.J., van Laere, A., Witters, R. et al. Purification and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Petunia hybrida . Plant Mol Biol 14, 93–102 (1990). https://doi.org/10.1007/BF00015658

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  • DOI: https://doi.org/10.1007/BF00015658

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