Ferrara P, Li C H
Int J Pept Protein Res. 1982 Mar;19(3):259-62.
Human beta-endorphin analogs with various chain lengths have been investigated for their potency in displacing tritiated dihydromorphine and Leu-enkephalin binding in rat brain membrane preparations. It was found that the reduction of chain length from residues 1-31 to 1-5 led to a gradual loss of preference for the morphined receptor. In addition, the extension of the chain length of the Met-ekephalin segment to the COOH-terminal glutamic acid modified the binding of the NH2-terminal sequence to the enkephalin receptor. The fact that camel beta-endorphin is more potent in displacing the two tritiated primary ligands than the human hormone is also reported herein.
人们已经研究了具有不同链长的人β-内啡肽类似物在大鼠脑膜制剂中取代氚化二氢吗啡和亮氨酸脑啡肽结合的效力。研究发现，链长从1-31个残基减少到1-5个残基会导致对吗啡受体的偏好逐渐丧失。此外，甲硫氨酸脑啡肽片段的链长延伸至COOH末端谷氨酸会改变NH2末端序列与脑啡肽受体的结合。本文还报道了骆驼β-内啡肽在取代两种氚化主要配体方面比人β-内啡肽更有效的事实。
