Antioxidant Peptides with Angiotensin Converting Enzyme Inhibitory Activities and Applications for Angiotensin Converting Enzyme Purification
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- 作者：Wen-Chi Hou ; Hsien-Jung Chen ; and Yaw-Huei Lin
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2003
- 出版时间：March 12, 2003
- 年：2003
- 卷：51
- 期：6
- 页码：1706 - 1709
- 全文大小：79K
- 年卷期：v.51,no.6(March 12, 2003)
- ISSN：1520-5118
文摘
Five commercial peptides, namely, reduced glutathione (GSH), oxidized glutathione (GSSG),carnosine, homocarnosine, and anserine, were used to test angiotensin converting enzyme inhibitory(ACEI) activities using N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly (FAPGG) as a substrate. All of these peptidesshowed dose-dependent ACEI activities. Using 50% inhibition (IC50) of captopril as 0.00781 
M forthe reference, the IC50 values of GSH, carnosine, homocarnosine, and anserine were determined tobe 32.4 M, 5.216 mM, 6.147 mM, and 6.967 mM, respectively. GSH or carnosine showed mixednoncompetitive inhibition against ACE. When 0.0164 mM GSH or 0.4098 mM carnosine was added,the apparent inhibition constant (Ki) was 49.7 M or 3.899 mM, respectively. Commercial glutathione-Sepharose 4 fast flow, GSH-coupled CNBr-activated and GSH-coupled EAH-activated Sepharosegels were used for ACE purification. Commercial ACE could be adsorbed only by EAH-coupled GSHgels and eluted off the gels by increasing salt concentrations. These EAH-coupled GSH gels mightbe developed as affinity aids for ACE purification.Keywords: Angiotensin converting enzyme (ACE); glutathione; N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly(FAPGG); peptide; EAH-activated gel
M forthe reference, the IC50 values of GSH, carnosine, homocarnosine, and anserine were determined tobe 32.4 M, 5.216 mM, 6.147 mM, and 6.967 mM, respectively. GSH or carnosine showed mixednoncompetitive inhibition against ACE. When 0.0164 mM GSH or 0.4098 mM carnosine was added,the apparent inhibition constant (Ki) was 49.7 M or 3.899 mM, respectively. Commercial glutathione-Sepharose 4 fast flow, GSH-coupled CNBr-activated and GSH-coupled EAH-activated Sepharosegels were used for ACE purification. Commercial ACE could be adsorbed only by EAH-coupled GSHgels and eluted off the gels by increasing salt concentrations. These EAH-coupled GSH gels mightbe developed as affinity aids for ACE purification.Keywords: Angiotensin converting enzyme (ACE); glutathione; N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly(FAPGG); peptide; EAH-activated gel