L-Arginine suppresses aggregation of recombinant growth hormones in refolding process from E-Coli inclusion bodies

被引：28

作者：

Bajorunaite, Egle ^{[1
]}

Sereikaite, Jolanta ^{[1
]}

Bumelis, Vladas-Algirdas ^{[1
]}

机构：

[1] Vilnius Gediminas Tech Univ, Fac Fundamental Sci, Dept Chem & Bioengn, LT-10223 Vilnius 40, Lithuania

来源：

PROTEIN JOURNAL | 2007年 / 26卷 / 08期

关键词：

L-Arginine; recombinant growth hormones; refolding; aggregation;

D O I：

10.1007/s10930-007-9096-x

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：

L-Arginine was used to suppress the aggregation of recombinant mink and porcine growth hormones in the refolding process from E. coli inclusion bodies by solubilization-dilution protocol at high protein concentration and pH 8.0. The influence of L-arginine concentration on the renaturation yield of both proteins was investigated. L-Arginine effectively suppressed the precipitation of growth hormones during dilution, but did not inhibit soluble oligomers formation. The results of mink and porcine growth hormones purification from 4 g of biomass are presented.

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收藏

页码：547 / 555

页数：9

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