Ueno A, Arakaki N, Inoue H, Oribe T, Takeda Y
Biochem Biophys Res Commun. 1984 Aug 16;122(3):1179-85. doi: 10.1016/0006-291x(84)91216-6.
Insulin-stimulating peptide was isolated from a tryptic digest of bovine serum albumin by gel permeation, SP Sephadex column chromatography, reversed phase HPLC and cation-exchange HPLC. This peptide, with a molecular weight of about 8,400, had no insulin-like activity by itself, but enhanced fatty acid synthesis from glucose in rat adipose tissue explants in the presence of suboptimal concentrations of insulin. It also stimulated the effect of insulin on CO2 production from glucose in rat adipocytes, without affecting insulin binding. These stimulations were dose-dependent and were observed at concentrations of more than 2 X 10(-7) M peptide only in the presence of a suboptimal concentration of insulin.
通过凝胶渗透、SP Sephadex柱色谱、反相高效液相色谱和阳离子交换高效液相色谱从牛血清白蛋白的胰蛋白酶消化物中分离出胰岛素刺激肽。这种分子量约为8400的肽本身没有胰岛素样活性，但在胰岛素浓度次优的情况下，能增强大鼠脂肪组织外植体中葡萄糖的脂肪酸合成。它还能刺激胰岛素对大鼠脂肪细胞中葡萄糖产生二氧化碳的作用，而不影响胰岛素结合。这些刺激作用呈剂量依赖性，且仅在胰岛素浓度次优时，在肽浓度超过2×10⁻⁷ M时才观察到。
