Broothaerts W J, van Laere A, Witters R, Préaux G, Decock B, van Damme J, Vendrig J C
Laboratory of Plant Physiology, Katholieke Universiteit Leuven, Belgium.
Plant Mol Biol. 1990 Jan;14(1):93-102. doi: 10.1007/BF00015658.
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 micrograms 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.
我们报道了三种花柱糖蛋白的分离及N端氨基酸测序，它们与矮牵牛的三个S（自交不亲和）等位基因分离。S糖蛋白主要在雌蕊上部表达，且在花发育过程中浓度不断增加。通过伴刀豆球蛋白A-琼脂糖和阳离子交换快速蛋白质液相色谱相结合的方法对糖蛋白进行了纯化。从花柱提取物中回收的S糖蛋白量为每个花柱0.5至1.6微克，这是通过简化分析方法回收量的40-60%。S1-、S2-和S3-糖蛋白的N端氨基酸序列在十五个N端残基内显示出同源性。这些氨基酸序列与之前发表的来自烟草和秘鲁番茄的S糖蛋白序列进行了比较。
