Yeh S C, Hsieh H M, Huang P C
Department of Life Sciences, National Tsing Hua University Hsin-Chu, Taiwan, ROC.
DNA Seq. 1995;5(3):141-4. doi: 10.3109/10425179509029353.
Using oligonucleotides with highly conserved cysteine-rich codons as probes, we isolated from a lambda YES Arabidopsis thaliana cDNA library two different sequences, each encodes an unique protein. These proteins, hereby designated as AtMT-q (AtMT-2) and AtMT-k (AtMT-1), are characteristic of metallothionein, carrying 13 and 14 cysteines in a total of 45 and 81 amino acids, respectively.
我们使用富含半胱氨酸的高度保守密码子的寡核苷酸作为探针，从λYES拟南芥cDNA文库中分离出两个不同的序列，每个序列都编码一种独特的蛋白质。这些蛋白质，在此命名为AtMT-q（AtMT-2）和AtMT-k（AtMT-1），是金属硫蛋白的特征，分别在总共45个和81个氨基酸中含有13个和14个半胱氨酸。
