Seidah N G, Lis M, Gianoulakis C, Routhier R, Benjannet S, Schiller P W, Chretien M
Can J Biochem. 1977 Jan;55(1):35-40. doi: 10.1139/o77-006.
Sheep beta-lipotropin (beta-LPH) (sequence 1-91) was selectively cleaved with trypsin after blocking the epsilon-amino groups of lysine with citraconic anhydride. The resulting peptides were purified by a combination of cation-exchange chromatography and high-voltage electrophoresis. The purified fragments were then tested for their morphine-like activity in the mouse vas deferens bioassay. The active peptides were 61-91 and 61-80 were about as active as the synthetic methionine-enkephalin, and in turn these were about 100 times more active than beta-LPH itself. The inhibition of electrically stimulated mouse vas deferens by these peptides is reversed by naloxone, and suggests a competitive character of interaction. It is thus concluded that the active core for the morphine like activity in the mouse vas deferens bioassay is the fragment 61-65 of beta-LPH.
用柠康酸酐封闭赖氨酸的ε-氨基后，用胰蛋白酶对绵羊β-促脂素（β-LPH）（序列1 - 91）进行选择性切割。通过阳离子交换色谱法和高压电泳相结合的方法对所得肽段进行纯化。然后在小鼠输精管生物测定中测试纯化片段的吗啡样活性。活性肽61 - 91和61 - 80的活性与合成的甲硫氨酸脑啡肽相当，而它们的活性又比β-LPH本身高约100倍。这些肽对电刺激的小鼠输精管的抑制作用可被纳洛酮逆转，提示存在竞争性相互作用。因此得出结论，在小鼠输精管生物测定中，具有吗啡样活性的活性核心是β-LPH的61 - 65片段。
