HPLC-ESI-MS对珠蛋白酶解液中的血管紧张素I转换酶抑制肽的分离鉴定

Isolation and Identification of Angiotensin I-converting Enzyme Inhibitory Peptide Derived from Peptic Globin Hydrolysate by HPLC-ESI-MS

本实验利用ESI-MS/MS对反相高效液相色谱分离的具有血管紧张素I转换酶(ACE)抑制活性的珠蛋白小肽的结构进行鉴定。结果表明:此肽的序列为Val-Val-Tyr-Pro-Trp-Thr(VVYPWT),位于猪的血红蛋白β链的34-39氨基酸序列片断,它对ACE有很好的抑制活性,其IC50为6.02μmol/L。

This paper described isolation and identification of angiotensin I-converting enzyme （ACE） inhibitory peptide derived from the peptic globin hydrolysate. After the isolation of ACE inhibitory peptide with reversed-phase high-performance liquid chromatography （RP-HPLC） on Cls column, one active fraction was obtained, The amino acid sequence was identified by electrospray ionization tandem mass spectrometry （ESI-MS-MS）. The results showed that this peptide is ValVaI-Tyr-Pro-Trp-Thr（VVYPWT）, corresponding to the 34-39 fragment of the β chain of porcine hemoglobin, with IC50 value as 6.02 μmol/L.