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马L-铁蛋白在大肠杆菌中的克隆、表达及特性分析

Cloning, expression and characterization of horse L-ferritin in Escherichia coli.

作者信息

Takeda S, Ohta M, Ebina S, Nagayama K

机构信息

Protein Array Project, ERATO, JRDC, Tsukuba, Japan.

出版信息

Biochim Biophys Acta. 1993 Aug 19;1174(2):218-20. doi: 10.1016/0167-4781(93)90121-s.

Abstract

Horse L-ferritin cDNA was cloned from horse liver, and the base sequence was determined. The L-ferritin was expressed using pTZ18U encoding lac promoter, and found to possess an additional 8-amino acid sequence at the N-terminus as compared with commercially obtained horse spleen (natural) ferritin. It was determined that there was Pro at position 94 in both the recombinant and natural L-ferritin, although it was previously reported that Leu was in this position in the natural species. Transmission electron microscopy showed that this recombinant ferritin formed a 24-mer shell.

摘要

从马肝脏中克隆出马L-铁蛋白cDNA,并测定了其碱基序列。使用编码lac启动子的pTZ18U表达L-铁蛋白,发现与市售马脾(天然)铁蛋白相比,其N端有一个额外的8个氨基酸序列。确定重组L-铁蛋白和天然L-铁蛋白的第94位均为脯氨酸,尽管此前报道天然物种中该位置为亮氨酸。透射电子显微镜显示该重组铁蛋白形成了一个24聚体外壳。

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