Veretennikova N I, Chipens G I, Nikiforovich G V, Betinsh Y R
Int J Pept Protein Res. 1981 Apr;17(4):430-5. doi: 10.1111/j.1399-3011.1981.tb02011.x.
Structure-function and conformational studies of the molecule of phagocytosis-stimulating tetrapeptide tuftsin permitted the conclusion that among products resulting from splitting of H-chain of IgG Human EU by trypsin, besides tuftsin (sequence 289-292), tuftsin-like tetrapeptide Gly-Gln-Pro-Arg may be also present; theoretical conformational analysis shows a considerable similarity of spatial arrangement of this tetrapeptide and tuftsin which testifies in favour of potential tuftsin-like activity of the tetrapeptide. Gly-Gln-Pro-Arg was synthesized and its phagocytosis stimulating activity was found equal to that of tuftsin.
对促吞噬四肽tuftsin分子的结构功能和构象研究得出结论:在胰蛋白酶裂解人IgG重链产生的产物中,除了tuftsin(序列289 - 292)外,可能还存在类tuftsin四肽Gly - Gln - Pro - Arg;理论构象分析表明,该四肽与tuftsin的空间排列有相当大的相似性,这证明该四肽具有潜在的类tuftsin活性。合成了Gly - Gln - Pro - Arg,并发现其促吞噬活性与tuftsin相当。