Recombinant human nerve growth factor for clinical trials: protein expression, purification, stability and characterisation of binding to infusion pumps

被引:16
作者
Allen, SJ [1 ]
Robertson, AGS
Tyler, SJ
Wilcock, GK
Dawbarn, D
机构
[1] Univ Bristol, Mol Neurobiol Unit, Res Ctr Neuroendocrinol, Bristol BS2 8HW, Avon, England
[2] Univ Bristol, Frenchay Hosp, Dept Care Elderly, Bristol BS16, Avon, England
来源
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS | 2001年 / 47卷 / 03期
基金
英国惠康基金; 英国医学研究理事会;
关键词
Alzheimer's disease; baculovirus; infusion pump; nerve growth factor (NGF); stability;
D O I
10.1016/S0165-022X(01)00134-8
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Nerve growth factor (NGF) has been suggested to be of therapeutic benefit to patients with Alzheimer's disease. One of the early changes in this disease is a loss of cholinergic function within the brain, and NGF is able to rescue cholinergic neurons both in vitro and in vivo. We describe the production of recombinant human beta -NGF (rhNGF), using baculovirus infection of insect cells; its purification, formulation and subsequent stability for use in clinical trials. Tests were also carried out to monitor release of protein from infusion pumps and catheters for intracerebroventricular administration (icv). Initial problems with non-specific binding were overcome using a blocking formula. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:239 / 255
页数:17
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