Nirasawa S, Masuda Y, Nakaya K, Kurihara Y
Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
Gene. 1996 Nov 28;181(1-2):225-7. doi: 10.1016/s0378-1119(96)00465-9.
A cDNA clone encoding a heat-stable sweet protein, mabinlin II (MAB), was isolated and sequenced. The encoded precursor to MAB was composed of 155 amino acid (aa) residues, including a signal sequence of 20 aa, an N-terminal extension peptide of 15 aa, a linker peptide of 14 aa and one residue of C-terminal extension. Comparison of the proteolytic cleavage sites during post-translational processing of MAB precursor with those of like 2S seed-storage proteins of Arabidopsis thaliana, Brassica napus and Bertholletia excelsa shows that the three individual cleavage sites between respective species are conserved.
分离并测序了一个编码热稳定甜味蛋白马槟榔II（MAB）的cDNA克隆。MAB的编码前体由155个氨基酸残基组成，包括一个20个氨基酸的信号序列、一个15个氨基酸的N端延伸肽、一个14个氨基酸的连接肽和一个C端延伸残基。将MAB前体翻译后加工过程中的蛋白水解切割位点与拟南芥、甘蓝型油菜和巴西坚果的类似2S种子贮藏蛋白的切割位点进行比较，结果表明各物种之间的三个独立切割位点是保守的。
