一种在纯化过程中分离胰岛素样生长因子1和2的有效方法。

An effective method for the separation of insulin-like growth factors 1 and 2 during the purification process.

作者信息

Tally M, Florell K, Enberg G

机构信息

Department of Endocrinology, Karolinska Institutet, Stockholm, Sweden.

出版信息

Biosci Rep. 1988 Jun;8(3):293-7. doi: 10.1007/BF01115047.

DOI:10.1007/BF01115047

PMID:3207863

Abstract

The separation of human insulin-like growth factors hIGF-1 and hIGF-2 was greatly improved by an additional purification step using the cation exchanger Mono-S (FPLC) compared to previous studies. Cross-reactions between hIGF-1 and hIGF-2 were strongly reduced. The more highly purified hIGF-1 had a cross-reaction of less than 1% in the RIA for hIGF-2, and was equivalent to recombinant hIGF-1. The pure hIGF-2 had a cross-reaction of less than 1% in the RIA for hIGF-1. In the human placental hIGF-2 radioreceptor assay, the hIGF-1 polypeptide completed less than 1% with hIGF-2 when the type 1 IGF receptor was blocked with insulin.

摘要

与先前的研究相比，使用阳离子交换剂Mono-S（快速蛋白质液相色谱法）进行额外的纯化步骤后，人胰岛素样生长因子hIGF-1和hIGF-2的分离得到了极大改善。hIGF-1和hIGF-2之间的交叉反应被大幅降低。纯化程度更高的hIGF-1在hIGF-2的放射免疫分析中的交叉反应小于1%，且等同于重组hIGF-1。纯hIGF-2在hIGF-1的放射免疫分析中的交叉反应小于1%。在人胎盘hIGF-2放射受体分析中，当1型胰岛素样生长因子受体被胰岛素阻断时，hIGF-1多肽与hIGF-2的竞争完成率小于1%。