کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2007854 | 1066387 | 2006 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin](/preview/png/2007854.png)
Animal blood is potentially an untapped source of drugs and value-added food production. More than 400 million pigs are slaughtered each year but porcine blood is usually discarded in China. This study describes the isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from porcine hemoglobin. The most active hydrolysate was obtained from the peptic digestion of porcine hemoglobin. After the purification of ACE-inhibitory peptides with Sephadex LH-20 gel chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) on C18 column, two active fractions were obtained. They were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). They were LGFPTTKTYFPHF and VVYPWT, corresponding to the 34–46 fragment of the α chain and the 34–39 fragment of the β chain of porcine hemoglobin, with IC50 values of 4.92 and 6.02 μM, respectively. They were the first found from porcine hemoglobin; in particular, LGFPTTKTYFPHF was a novel ACE-inhibitory peptide. In addition, the purified ACE inhibitors both competitively inhibited ACE, and maintained inhibitory activity even after incubation with gastrointestinal proteases. This suggests that these peptides might have a potential antihypertensive effect.
Journal: Peptides - Volume 27, Issue 11, November 2006, Pages 2950–2956