Sardinia M F, Hanesworth J M, Krebs L T, Harding J W
Department of Veterinary and Comparative Anatomy, Pharmacology, and Physiology, Washington State University, Pullman 99164-6520.
Peptides. 1993 Sep-Oct;14(5):949-54. doi: 10.1016/0196-9781(93)90071-n.
The ability of angiotensin IV (AIV) analogs to compete for [125I]AIV binding in heat-treated bovine adrenal membranes was examined. Angiotensin IV displayed a Ki of 2.63 +/- 0.12 nM. Peptides containing mono-substitutions with glycine or the corresponding D-amino acid in positions one, two, or three possessed K(i)s greater than 100 nM. Conversely, substitutions at positions four, five, and six produced peptides with Kis less than 8 nM. These data suggest that the N-terminal domains of the AIV peptide are critical for receptor binding, while the C-terminal domains play a less decisive role in receptor specificity.
研究了血管紧张素IV（AIV）类似物在热处理的牛肾上腺膜中竞争[125I]AIV结合的能力。血管紧张素IV的Ki值为2.63±0.12 nM。在第1、2或3位含有甘氨酸或相应D-氨基酸单取代的肽，其K(i)值大于100 nM。相反，在第4、5和6位的取代产生的肽，其Ki值小于8 nM。这些数据表明，AIV肽的N端结构域对受体结合至关重要，而C端结构域在受体特异性中起的作用较小。
