牛初乳中胰岛素样生长因子-1的纯化及部分序列分析
Purification and partial sequence analysis of insulin-like growth factor-1 from bovine colostrum.
作者信息
Francis G L, Read L C, Ballard F J, Bagley C J, Upton F M, Gravestock P M, Wallace J C
出版信息
Biochem J. 1986 Jan 1;233(1):207-13. doi: 10.1042/bj2330207.
Abstract
Growth-promoting activity in bovine colostrum has been detected as the capacity to stimulate protein synthesis in L6 myoblasts. By using this assay as a measure of bioactivity, a growth factor has been purified to near homogeneity from centrifuged colostrum by a series of steps including acid extraction, chromatography on sulphopropyl-Sephadex, followed by adsorption to, and elution from, C18 columns using acetonitrile and propan-1-ol gradients. The purified growth factor has a low solubility at neutral and alkaline pH and has an Mr of 7800 by gel-permeation chromatography. Sequence analysis of the first 30 amino acids from the N-terminus indicated complete identity in this region with human insulin-like growth factor-1. Accordingly we conclude that the purified growth factor is bovine insulin-like growth factor-1.
摘要
牛初乳中的促生长活性已被检测为刺激L6成肌细胞中蛋白质合成的能力。通过使用该测定法作为生物活性的量度，一种生长因子已通过一系列步骤从离心初乳中纯化至接近均一，这些步骤包括酸提取、在磺丙基-葡聚糖凝胶上进行色谱分离，然后使用乙腈和丙-1-醇梯度吸附到C18柱上并从C18柱上洗脱。纯化的生长因子在中性和碱性pH下溶解度低，通过凝胶渗透色谱法测得其Mr为7800。对N端前30个氨基酸的序列分析表明，该区域与人类胰岛素样生长因子-1完全相同。因此，我们得出结论，纯化的生长因子是牛胰岛素样生长因子-1。
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