Ng F M, Bornstein J, Pullin C E, Bromley J O, Macaulay S L
Diabetes. 1980 Oct;29(10):782-7. doi: 10.2337/diacare.20.10.782.
A series of synthetic peptides corresponding to the amino-terminal sequence of human growth hormone (hGH) has been studied for insulin-potentiating effects using three different bioassay systems: (1) intravenous insulin tolerance tests, (2) insulin binding to specific receptors of hepatic plasma membranes and isolated hepatocytes, and (3) modulation of insulin-dependent glycogen synthase and glycogen phosphorylase in muscle and adipose tissue. The results establish that the minimum active sequence is the hexapeptide (hGH 8-13) containing H2N-Arg-Leu-Phe-Asp-Asn-Ala-COOH and strongly indicate that the insulin-potentiating action of the active peptides is to increase the binding of insulin to specific receptors and thus modulate the action of glycogen synthase and phosphorylase, producing hypoglycemia as the result of increased glycogen storage in liver, muscle, and adipose tissue.
利用三种不同的生物测定系统，对一系列与人生长激素（hGH）氨基末端序列相对应的合成肽进行了胰岛素增强作用的研究：（1）静脉内胰岛素耐量试验；（2）胰岛素与肝细胞膜及分离的肝细胞的特异性受体结合；（3）调节肌肉和脂肪组织中胰岛素依赖性糖原合酶和糖原磷酸化酶。结果表明，最小活性序列是包含H2N-Arg-Leu-Phe-Asp-Asn-Ala-COOH的六肽（hGH 8-13），并强烈表明活性肽的胰岛素增强作用是增加胰岛素与特异性受体的结合，从而调节糖原合酶和磷酸化酶的作用，由于肝、肌肉和脂肪组织中糖原储存增加而导致低血糖。
