EXPRESSION, PURIFICATION AND BINDING TO THE RECEPTOR OF HUMAN INSULIN-LIKE GROWTH FACTOR-II

被引：0

作者：

MIYAGISHIMA, T

GASA, S

HONKE, K

SAKAI, M

NISHI, S

YAMAMOTO, M

NISHIKAWA, K

MIYAZAKI, T

MAKITA, A

机构：

[1] SAPPORA MED UNIV,SCH MED,DEPT CHEM,CHUO KU,SI W17,SAPPORO 060,JAPAN

[2] HOKKAIDO UNIV,SCH MED,DEPT INTERNAL MED 3,SAPPORO,HOKKAIDO 060,JAPAN

[3] HOKKAIDO UNIV,SCH MED,DEPT BIOCHEM,SAPPORO,HOKKAIDO 060,JAPAN

[4] KANAZAWA MED UNIV,DEPT BIOCHEM,ISHIKAWA 92002,JAPAN

[5] NATL DEF MED COLL,BIOCHEM 2 LAB,TOKOROZAWA,SAITAMA 359,JAPAN

[6] HOKKAIDO UNIV,SCH MED,INST CANC,BIOCHEM LAB,SAPPORO,HOKKAIDO 060,JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1203卷 / 01期

关键词：

INSULIN-LIKE GROWTH FACTOR-II; GENE EXPRESSION; RECEPTOR; PROTEIN PURIFICATION; (HUMAN);

D O I：

10.1016/0167-4838(93)90050-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human insulin-like growth factor II (IGF-II) was expressed as a fused protein with 14 additive amino acids in Escherichia coli with a high yield by an expression system using T7 RNA polymerase. Purification of the expressed protein was simply performed using only differential ultrafiltrations, giving a homogeneous preparation upon polyacrylamide gel electrophoresis and high-performance liquid chromatography. The expressed peptide was reacted with a monoclonal antibody raised against native IGF-II on a blotted membrane. Furthermore, the peptide was bound to IGF-II receptor in solubilized rat fetus membrane, though the affinity was slightly inferior to that of native IGF-II. In addition, fusion IGF-II immobilized on a gel matrix was useful for one-step purification of the IGF-II receptor with a high yield from solubilized rat fetus membranes.

引用

页码：155 / 161

页数：7

共 23 条

[1] EXPRESSION OF A HUMAN INSULIN-LIKE GROWTH FACTOR-II CDNA IN NIH-3T3 CELLS [J].