Identification of the heparin-binding domain of TNF-alpha and its use for efficient TNF-alpha purification by heparin-Sepharose affinity chromatography

被引：20

作者：

Kenig, Maja ^{[1
]}

Gaberc-Porekar, Vladka ^{[2
]}

Fonda, Irena ^{[2
]}

Menart, Viktor ^{[1
,2
]}

机构：

[1] Lek Pharmaceut Dd, SL-1526 Ljubljana, Slovenia

[2] Natl Inst Chem, SL-1001 Ljubljana, Slovenia

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2008年 / 867卷 / 01期

关键词：

heparin-binding domain; TNF-alpha; affinity chromatography;

D O I：

10.1016/j.jchromb.2008.03.023

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The N-terminus of the trimeric TNF-alpha molecule comprises two basic arginines within the short amino-acid sequence VRSSSR, which is here shown to be essential for binding of TNF-alpha to heparin-Sepharose. Mixed trimers containing full-length and Delta N6-truncated subunits revealed a single VRSSSR sequence to be sufficient to achieve binding. On the basis of this newly identified heparin-binding domain, a new method for efficient purification of TNF-alpha is described. Affinity chromatography on heparin-Sepharose was introduced as a key step for highly purified TNF-alpha at a high yield. With minor modifications, this procedure can be used for TNF-alpha analogues that have full-length N-termini, as shown for the less toxic analogue LK-805. (C) 2008 Elsevier B.V. All rights reserved.

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收藏

页码：119 / 125

页数：7

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