HIGH-LEVEL SYNTHESIS IN ESCHERICHIA-COLI OF SHORTENED AND FULL-LENGTH HUMAN ACIDIC FIBROBLAST GROWTH-FACTOR AND PURIFICATION IN A FORM STABLE IN AQUEOUS-SOLUTIONS

被引：68

作者：

ZAZO, M ^{[1
]}

LOZANO, RM ^{[1
]}

ORTEGA, S ^{[1
]}

VARELA, J ^{[1
]}

DIAZOREJAS, R ^{[1
]}

RAMIREZ, JM ^{[1
]}

GIMENEZGALLEGO, G ^{[1
]}

机构：

[1] CSIC,CTR INVEST BIOL,VELAZQUEZ 144,E-28006 MADRID,SPAIN

来源：

GENE | 1992年 / 113卷 / 02期

关键词：

RECOMBINANT DNA; MESSENGER RNA SECONDARY STRUCTURES; POLYCISTRONIC MESSENGER TRANSLATION; INITIATOR METHIONINE PROCESSING; PROTEIN MODIFICATION BY REVERSED-PHASE CHROMATOGRAPHY;

D O I：

10.1016/0378-1119(92)90400-J

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

A highly efficient expression for human acidic fibroblast growth factor (aFGF) has been assembled to direct the synthesis of both shortened and native full-length aFGF. The full-length aFGF-154 form of the protein had not been produced before in Escherichia coli by genetic engineering, and is obtained with its initiator methionine removed. The high production of the aFGF allows one to circumvent the use of reversed-phase chromatography (RPC) during the purification procedure. Here, it is shown that RPC, routinely used to obtain pure preparations of recombinant aFGF, modifies its chemical and physical properties in an unfavorable manner.

引用

页码：231 / 238

页数：8

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