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一种碘化蛋白质(β神经生长因子)的改进纯化方法。

Improved procedure for the purification of an iodinated protein: beta nerve growth factor.

作者信息

Ennulat D J, Stach R W

出版信息

Neurochem Res. 1985 Jul;10(7):1009-14. doi: 10.1007/BF00964636.

Abstract

An improved procedure for the isolation of iodinated beta Nerve Growth Factor (125I-beta NGF) has been devised. Use of Centricon microconcentrators (Amicon) has allowed the facile and efficient recovery of ultrapure 125I-beta NGF in high yields. Centricon microconcentrators are supplied with two molecular weight cutoffs of 10 K and 30 K daltons. beta NGF is a basic protein with a molecular weight of 26 K daltons. It is therefore possible to filter the 125I-beta NGF through the 30 K filter (30 K Filtrate) leaving behind any aggregates or reactants greater than 30 K while the 125I-beta NGF can be retained and concentrated on the 10 K filter (10 K Retentate). Any free 125I is easily removed, passing through the 10 K filter and then being discarded. In this way 125I-beta NGF can be easily purified.

摘要

已设计出一种改进的碘化β神经生长因子(¹²⁵I-βNGF)分离方法。使用Centricon微浓缩器(密理博公司)能够以高产率轻松且高效地回收超纯¹²⁵I-βNGF。Centricon微浓缩器提供10K和30K道尔顿两种分子量截留值。βNGF是一种分子量为26K道尔顿的碱性蛋白。因此,¹²⁵I-βNGF可通过30K过滤器过滤(30K滤液),从而将任何大于30K的聚集体或反应物留在后面,而¹²⁵I-βNGF可被保留并浓缩在10K过滤器上(10K截留物)。任何游离的¹²⁵I很容易被除去,它会通过10K过滤器然后被丢弃。通过这种方式,¹²⁵I-βNGF能够轻松得到纯化。

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