Zhao Q, Garreau I, Sannier F, Piot J M
Laboratoire de Génie Protéique, Université de La Rochelle, France.
Biopolymers. 1997;43(2):75-98. doi: 10.1002/(SICI)1097-0282(1997)43:2<75::AID-BIP2>3.0.CO;2-X.
Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors. Two peptides, VV-hemorphin-7 and LVV-hemorphin-7, were resolved by a combination of size exclusion and reversed phase HPLC. A new spectroscopic method based on the second order derivative spectra analysis of aromatic amino acids has been developed. This method allows qualitative and quantitative evaluation of hemorphins generated by peptic hemoglobin hydrolysis. Using this method, a kinetic study of hemorphins appearance has been undertaken. In this paper, we also evidenced the generation of VV-hemorphin-7 from globin by peritoneal macrophages. In regard to this result, the putative physiological role of hemorphins is discussed.
对血红蛋白胃蛋白酶水解产物的研究揭示了存在对阿片受体具有亲和力的生物活性肽。通过尺寸排阻和反相高效液相色谱相结合的方法分离出了两种肽,即VV-血啡肽-7和LVV-血啡肽-7。已开发出一种基于芳香族氨基酸二阶导数光谱分析的新光谱方法。该方法可对胃蛋白酶水解血红蛋白产生的血啡肽进行定性和定量评估。利用该方法,对血啡肽的生成进行了动力学研究。在本文中,我们还证明了腹膜巨噬细胞可从珠蛋白生成VV-血啡肽-7。针对这一结果,讨论了血啡肽可能的生理作用。