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Purification and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Petunia hybrida
Authors:Wim J Broothaerts  André van Laere  Raf Witters  Gisèle Préaux  Benny Decock  Jozef van Damme  Jan C Vendrig
Institution:(1) Laboratory of Plant Physiology, Katholieke Universiteit Leuven (K.U. Leuven), Kardinaal Mercierlaan 92, B-3030 Heverlee, Belgium;(2) Laboratory of Developmental Biology, Katholieke Universiteit Leuven (K.U. Leuven), Kardinaal Mercierlaan 92, B-3030 Heverlee, Belgium;(3) Laboratory of Biochemistry, K.U. Leuven, Dekenstraat 6, B-3000, Leuven, Belgium;(4) Rega Institute for Medical Research, K.U. Leuven, Minderbroedersstraat 10, B-3000, Leuven, Belgium
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 mgrg 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:N-terminal amino acid sequence  Petunia  S-allele  self-incompatibility  style
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