PURIFICATION AND ANALYSIS OF THE STRUCTURE OF ALPHA-GALACTOSIDASE FROM ESCHERICHIA-COLI
PURIFICATION AND ANALYSIS OF THE STRUCTURE OF ALPHA-GALACTOSIDASE FROM ESCHERICHIA-COLI
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DOI：
10.1016/0006-291x(88)90584-0
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发表时间：
1988-02-29
影响因子：
3.1
通讯作者：
TSUCHIYA, T
中科院分区：
文献类型：
--
作者：
NAGAO, Y;NAKADA, T;TSUCHIYA, T
α-半乳糖苷酶是melA基因的产物，从含有携带melA的质粒的大肠杆菌菌株中纯化，该菌株过量产生α-半乳糖苷酶。半乳糖苷酶。表观分子量测定为50 kDa。测定了该酶的氨基酸组成。结果表明，该酶是一种亲水性酸性蛋白。我们对纯化的酶进行了20个循环的N-末端序列分析。这验证了melA基因的翻译起始位点和预测的N-末端序列。
.alpha.-Galactosidase, the product of the melA gene, was purified from a strain of Escherichia coli harboring a plasmid carrying melA, which overproduced the .alpha.-galactosidase. An apparent molecular weight was determined to be 50 kDa. The amino acid composition of this enzyme was determined. The result indicates that this enzyme is a hydrophilic and acidic protein. We have subjected the purified enzyme to 20 cycles of N-terminal sequence analysis. This verified the translation start site of the melA gene and the predicted N-terminal sequence.