重组前原伴刀豆球蛋白A（洋刀豆）稳定但溶解度低。
Recombinant pre-pro-Concanavalin A (jack bean) is stable but of low solubility.
作者信息
Dincturk H B, Dunn A J, Jones D H
机构信息
Molecular Biology Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, SA2 8PP, UK.
出版信息
J Biosci. 2001 Dec;26(5):635-40. doi: 10.1007/BF02704761.
The cDNA for pre-pro-Concanavalin A (pre-pro-ConA) was cloned into the cytoplasmic expression vector pKK233-2 to give rise to pCONEXP2 which was used to express the lectin precursor. Pre-pro-ConA is stable and is not transposed and ligated to form the mature protein. No signal peptide removal is observed. The solubility of pre-pro-ConA could not be increased by guanidine hydrochloride denaturation/dilution treatment.
将伴刀豆球蛋白A前体（pre-pro-ConA）的cDNA克隆到细胞质表达载体pKK233-2中，构建出pCONEXP2，用于表达凝集素前体。pre-pro-ConA是稳定的，不会发生转位和连接以形成成熟蛋白。未观察到信号肽的去除。盐酸胍变性/稀释处理无法提高pre-pro-ConA的溶解度。
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