Root-Bernstein R S, Westall F C
Brain Res Bull. 1986 Oct;17(4):519-28. doi: 10.1016/0361-9230(86)90219-4.
We report results of chromatographic, pH titration and nuclear magnetic resonance (NMR) spectroscopy studies demonstrating that the bovine pineal antireproductive tripeptide, Thr-Ser-Lys (BPART), binds to luteinizing hormone-releasing hormone (LHRH) at a site comprised of LHRH 2-5 (His-Trp-Ser-Tyr). BPART and LHRH have been shown to be antagonists in vitro. The binding constant is ca. 2 X 10(3)/mole. An NMR study of fifty other peptide pairs demonstrates that the binding is sequence and residue specific. The binding provides evidence of the amino acid pairing hypothesis, and suggests the possibility of modulation of one peptide by directly binding with another peptide.
我们报告了色谱、pH滴定和核磁共振（NMR）光谱研究结果，这些结果表明牛松果体抗生殖三肽Thr-Ser-Lys（BPART）在由促黄体生成素释放激素（LHRH）的2-5位（His-Trp-Ser-Tyr）组成的位点与LHRH结合。BPART和LHRH在体外已被证明是拮抗剂。结合常数约为2×10³/摩尔。对其他五十对肽的NMR研究表明，这种结合具有序列和残基特异性。这种结合为氨基酸配对假说提供了证据，并表明了一种肽通过与另一种肽直接结合来进行调节的可能性。
