Takasaki C, Aimoto S, Takayanagi R, Ohashi M, Nawata H
Department of Chemistry, Faculty of Science, Tohoku University, Sendai, Japan.
Biochem Int. 1990 Sep;21(6):1059-64.
The specific binding of 125I-sarafotoxin S6b was observed in the microsomal fractions from porcine thoracic aorta, and two vasoconstrictive peptides with strikingly homologous structures, sarafotoxin (SRT) and endothelin (ET), interact with a common receptor of the vasculature. The order of the potency of an each endothelin or sarafotoxin analogue as a competitor against 125I-sarafotoxin S6b binding was ET-1 greater than ET-2 greater than SRT S6b greater than ET-3 much greater than SRT S6c. The hydrophobic carboxyl-terminal tail and intramolecular disulfide bridges are essential for the binding activity. In addition, Ser4, Ser5 and Lys9 seem to be important for the activity while the 6th residue does not affect the activity.
在猪胸主动脉微粒体部分观察到了125I-沙拉毒素S6b的特异性结合，并且两种具有惊人同源结构的血管收缩肽，即沙拉毒素（SRT）和内皮素（ET），与脉管系统的共同受体相互作用。每种内皮素或沙拉毒素类似物作为125I-沙拉毒素S6b结合竞争剂的效力顺序为：ET-1大于ET-2大于SRT S6b大于ET-3远大于SRT S6c。疏水的羧基末端尾巴和分子内二硫键对于结合活性至关重要。此外，丝氨酸4、丝氨酸5和赖氨酸9似乎对活性很重要，而第6个残基不影响活性。
