Oxidative folding of nerve growth factor can be mediated by the pro-peptide of neurotrophin-3

被引:14
|
作者
Hauburger, Anja
Kliemannel, Marco
Madsen, Peder
Rudolph, Rainer
Schwarz, Elisabeth
机构
[1] Univ Halle Wittenberg, Inst Biotechnol, D-06120 Halle, Germany
[2] Aarhus Univ, Dept Med Biochem, MIND Ctr, DK-8000 Aarhus C, Denmark
关键词
neurotrophins; nerve growth factor; neurotrophin-3; pro-form; oxidative folding;
D O I
10.1016/j.febslet.2007.07.063
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
We have previously shown that the pro-peptide of human nerve growth factor (NGF) facilitates oxidative folding of the mature part. For the analysis of functional specificities of the pro-peptides of NGF and the related neurotrophin-3 (NT-3) with respect to structure formation, chimeric proteins with swapped pro-peptides were generated. Neither the structure nor the stability of the mature domains was influenced by the heterologous pro-peptides. For the pro-peptide of NT-3 fused to the mature part of NGF, stabilization of the pro-peptide moiety by the NGF part was observed. Folding kinetics and renaturation yields of this chimeric protein were comparable to those of proNGF. Our results demonstrate functional interchangeability between the pro-peptides of NGF and NT-3 with respect to their role in assisting oxidative folding of the mature part. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:4159 / 4164
页数:6
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