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Volumn 239, Issue 6, 2014, Pages 933-940

Isolation of angiotensin I-converting enzyme inhibitor from pepsin hydrolysate of porcine hemoglobin

Author keywords

ACE inhibitory peptide; Amino acid sequence; Porcine hemoglobin; Purification

Indexed keywords

AMINO ACIDS; HEMOGLOBIN; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ION EXCHANGE; PEPTIDES; PURIFICATION;

EID: 84911987065     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-014-2290-0     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • COI: 1:CAS:528:DC%2BD28XpsVOisb4%3D
    • Lopez-Fandino R, Otte J, van Camp J (2006) Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int Dairy J 16(11):1277–1293. doi:10.1016/j.idairyj.2006.06.004
    • (2006) Int Dairy J , vol.16 , Issue.11 , pp. 1277-1293
    • Lopez-Fandino, R.1    Otte, J.2    van Camp, J.3
  • 2
    • 84866984624 scopus 로고    scopus 로고
    • The renin-angiotensin-aldosterone system in 2011: role in hypertension and chronic kidney disease
    • Silva ACSE, Flynn JT (2012) The renin-angiotensin-aldosterone system in 2011: role in hypertension and chronic kidney disease. Pediatr Nephrol 27(10):1835–1845. doi:10.1007/s00467-011-2002-y
    • (2012) Pediatr Nephrol , vol.27 , Issue.10 , pp. 1835-1845
    • Silva, A.C.S.E.1    Flynn, J.T.2
  • 3
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production
    • COI: 1:CAS:528:DC%2BD2sXlsVagt74%3D
    • Murray BA, FitzGerald RJ (2007) Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Design 13(8):773–791. doi:10.2174/138161207780363068
    • (2007) Curr Pharm Design , vol.13 , Issue.8 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 4
    • 0018622998 scopus 로고
    • Captopril in the treatment of clinical hypertension and cardiac failure
    • Atkinson AB, Robertson JI (1979) Captopril in the treatment of clinical hypertension and cardiac failure. Lancet 2(8147):836–839. doi:10.1016/S0140-6736(79)92186-X
    • (1979) Lancet , vol.2 , Issue.8147 , pp. 836-839
    • Atkinson, A.B.1    Robertson, J.I.2
  • 5
    • 1842478225 scopus 로고    scopus 로고
    • Hypotensive peptides from milk proteins
    • COI: 1:CAS:528:DC%2BD2cXjtFOrs7c%3D
    • FitzGerald RJ, Murray BA, Walsh DJ (2004) Hypotensive peptides from milk proteins. J Nutr 134(4):980s–988s
    • (2004) J Nutr , vol.134 , Issue.4 , pp. 980s-988s
    • FitzGerald, R.J.1    Murray, B.A.2    Walsh, D.J.3
  • 6
    • 84869167887 scopus 로고    scopus 로고
    • Evaluation of antihypertensive and antihyperlipidemic effects of bamboo shoot angiotensin converting enzyme inhibitory peptide in vivo
    • COI: 1:CAS:528:DC%2BC38XhsVyksrbL
    • Liu LL, Liu LY, Lu BY, Xia DZ, Zhang Y (2012) Evaluation of antihypertensive and antihyperlipidemic effects of bamboo shoot angiotensin converting enzyme inhibitory peptide in vivo. J Agric Food Chem 60(45):11351–11358. doi:10.1021/Jf303471f
    • (2012) J Agric Food Chem , vol.60 , Issue.45 , pp. 11351-11358
    • Liu, L.L.1    Liu, L.Y.2    Lu, B.Y.3    Xia, D.Z.4    Zhang, Y.5
  • 7
    • 0013848094 scopus 로고
    • Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom
    • COI: 1:CAS:528:DyaF2MXksVSnt7w%3D
    • Ferreira SH, e Silva MR (1965) Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom. Experientia 21(6):347–349
    • (1965) Experientia , vol.21 , Issue.6 , pp. 347-349
    • Ferreira, S.H.1    e Silva, M.R.2
  • 8
    • 0033812883 scopus 로고    scopus 로고
    • Utilization of bovine blood plasma proteins for the production of angiotensin I converting enzyme inhibitory peptides
    • Hyun CK, Shin HK (2000) Utilization of bovine blood plasma proteins for the production of angiotensin I converting enzyme inhibitory peptides. Process Biochem 36:6
    • (2000) Process Biochem , vol.36 , pp. 6
    • Hyun, C.K.1    Shin, H.K.2
  • 9
    • 0030830814 scopus 로고    scopus 로고
    • Analysis of peptides from bovine hemoglobin and tuna myoglobin enzymatic hydrolysate: use of HPLC with on-line second-order derivative spectroscopy for the characterization of biologically active peptides
    • Zhao Q, Le Coeur C, Piot JM (1997) Analysis of peptides from bovine hemoglobin and tuna myoglobin enzymatic hydrolysate: use of HPLC with on-line second-order derivative spectroscopy for the characterization of biologically active peptides. Analytica Chimica Acta 352:20
    • (1997) Analytica Chimica Acta , vol.352 , pp. 20
    • Zhao, Q.1    Le Coeur, C.2    Piot, J.M.3
  • 10
    • 0030843186 scopus 로고    scopus 로고
    • Opioid peptides derived from hemoglobin: hemorphins
    • COI: 1:CAS:528:DyaK2sXktFClu7k%3D
    • Zhao Q, Garreau I, Sannier F, Piot JM (1997) Opioid peptides derived from hemoglobin: hemorphins. Biopolymers 43(2):75–98. doi:10.1002/(SICI)1097-0282(1997)43:2<75:AID-BIP2>3.0.CO;2-X
    • (1997) Biopolymers , vol.43 , Issue.2 , pp. 75-98
    • Zhao, Q.1    Garreau, I.2    Sannier, F.3    Piot, J.M.4
  • 11
    • 84888052009 scopus 로고    scopus 로고
    • Simultaneous monitoring of temporal profiles of NO3, NO2 and O-3 by incoherent broadband cavity enhanced absorption spectroscopy for atmospheric applications
    • COI: 1:CAS:528:DC%2BC3sXhsVKnsL3L
    • Wu T, Coeur-Tourneur C, Dhont G, Cassez A, Fertein E, He XD, Chen WD (2014) Simultaneous monitoring of temporal profiles of NO3, NO2 and O-3 by incoherent broadband cavity enhanced absorption spectroscopy for atmospheric applications. J Quant Spectrosc Ra 133:199–205. doi:10.1016/j.jqsrt.2013.08.002
    • (2014) J Quant Spectrosc Ra , vol.133 , pp. 199-205
    • Wu, T.1    Coeur-Tourneur, C.2    Dhont, G.3    Cassez, A.4    Fertein, E.5    He, X.D.6    Chen, W.D.7
  • 12
    • 33746768459 scopus 로고    scopus 로고
    • Antioxidant properties of porcine blood protein before and after enzymatic hydrolysis
    • COI: 1:CAS:528:DC%2BD2MXhtVGqurvN
    • Wu KC, Lin ZY, Chiang SH, Chang CY (2004) Antioxidant properties of porcine blood protein before and after enzymatic hydrolysis. J Biomass Ener Soc China 23:6
    • (2004) J Biomass Ener Soc China , vol.23 , pp. 6
    • Wu, K.C.1    Lin, Z.Y.2    Chiang, S.H.3    Chang, C.Y.4
  • 14
    • 84862874630 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant and ACE inhibitory activities of egg white protein hydrolysate
    • COI: 1:CAS:528:DC%2BC38XjtFygs7o%3D
    • Chen C, Chi YJ, Zhao MY, Xu W (2012) Influence of degree of hydrolysis on functional properties, antioxidant and ACE inhibitory activities of egg white protein hydrolysate. Food Sci Biotechnol 21(1):27–34. doi:10.1007/s10068-012-0004-6
    • (2012) Food Sci Biotechnol , vol.21 , Issue.1 , pp. 27-34
    • Chen, C.1    Chi, Y.J.2    Zhao, M.Y.3    Xu, W.4
  • 15
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • COI: 1:CAS:528:DyaE3MXltVGgs78%3D
    • Cushman DW, Cheung HS (1971) Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem Pharmacol 20(7):1637–1648
    • (1971) Biochem Pharmacol , vol.20 , Issue.7 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 16
    • 78049417145 scopus 로고    scopus 로고
    • Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate
    • COI: 1:CAS:528:DC%2BC3cXhtlGmt73M
    • Lee JK, Jeon JK, Byun HG (2011) Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate. Food Chem 125(2):495–499. doi:10.1016/j.foodchem.2010.09.039
    • (2011) Food Chem , vol.125 , Issue.2 , pp. 495-499
    • Lee, J.K.1    Jeon, J.K.2    Byun, H.G.3
  • 17
    • 0020744658 scopus 로고
    • Sequence determination of eglin C using combined microtechniques of amino acid analysis, peptide isolation, and automatic Edman degradation
    • COI: 1:CAS:528:DyaL3sXktVamtLc%3D
    • Knecht R, Seemuller U, Liersch M, Fritz H, Braun DG, Chang JY (1983) Sequence determination of eglin C using combined microtechniques of amino acid analysis, peptide isolation, and automatic Edman degradation. Anal Biochem 130(1):65–71
    • (1983) Anal Biochem , vol.130 , Issue.1 , pp. 65-71
    • Knecht, R.1    Seemuller, U.2    Liersch, M.3    Fritz, H.4    Braun, D.G.5    Chang, J.Y.6
  • 18
    • 33746725357 scopus 로고    scopus 로고
    • Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates
    • COI: 1:CAS:528:DC%2BD28XotVeitbk%3D
    • Chang CY, Wu KC, Chiang SH (2007) Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates. Food Chem 100(4):1537–1543. doi:10.1016/j.foodchem.2005.12.019
    • (2007) Food Chem , vol.100 , Issue.4 , pp. 1537-1543
    • Chang, C.Y.1    Wu, K.C.2    Chiang, S.H.3
  • 19
    • 84877037320 scopus 로고    scopus 로고
    • Dipeptide synthesis in near-anhydrous organic media: long-term stability and reusability of immobilized Alcalase
    • COI: 1:CAS:528:DC%2BC3sXptFKqtb0%3D
    • Vossenberg P, Beeftink HH, Nuijens T, Quaedflieg PJLM, Stuart MAC, Tramper J (2013) Dipeptide synthesis in near-anhydrous organic media: long-term stability and reusability of immobilized Alcalase. J Mol Catal B-Enzym 93:23–27. doi:10.1016/j.molcatb.2013.03.014
    • (2013) J Mol Catal B-Enzym , vol.93 , pp. 23-27
    • Vossenberg, P.1    Beeftink, H.H.2    Nuijens, T.3    Quaedflieg, P.J.L.M.4    Stuart, M.A.C.5    Tramper, J.6
  • 20
    • 36048952787 scopus 로고    scopus 로고
    • Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate
    • COI: 1:CAS:528:DC%2BD2sXhtlajsL3M
    • Zhao YH, Li BF, Liu ZY, Dong SY, Zhao X, Zeng MY (2007) Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochem 42(12):1586–1591. doi:10.1016/j.procbio.2007.08.011
    • (2007) Process Biochem , vol.42 , Issue.12 , pp. 1586-1591
    • Zhao, Y.H.1    Li, B.F.2    Liu, Z.Y.3    Dong, S.Y.4    Zhao, X.5    Zeng, M.Y.6
  • 21
    • 34247619388 scopus 로고    scopus 로고
    • Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice
    • COI: 1:CAS:528:DC%2BD2sXkvFOitLk%3D
    • Zhong F, Liu JM, Ma JG, Shoemaker CF (2007) Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice. Food Res Int 40(6):661–667. doi:10.1016/j.foodres.2006.11.011
    • (2007) Food Res Int , vol.40 , Issue.6 , pp. 661-667
    • Zhong, F.1    Liu, J.M.2    Ma, J.G.3    Shoemaker, C.F.4
  • 22
    • 67349242954 scopus 로고    scopus 로고
    • Macroporous resin purification of grass carp fish (Ctenopharyngodon idella) scale peptides with in vitro angiotensin-I converting enzyme (ACE) inhibitory ability
    • COI: 1:CAS:528:DC%2BD1MXmvVyhtrg%3D
    • Zhang FX, Wang Z, Xu SY (2009) Macroporous resin purification of grass carp fish (Ctenopharyngodon idella) scale peptides with in vitro angiotensin-I converting enzyme (ACE) inhibitory ability. Food Chem 117(3):387–392. doi:10.1016/j.foodchem.2009.04.015
    • (2009) Food Chem , vol.117 , Issue.3 , pp. 387-392
    • Zhang, F.X.1    Wang, Z.2    Xu, S.Y.3
  • 23
    • 0034101865 scopus 로고    scopus 로고
    • Isolation and characterization of free radical scavenging activities peptides derived from casein
    • Suetsuna K, Ukeda H, Ochi H (2000) Isolation and characterization of free radical scavenging activities peptides derived from casein. J Nutr Biochem 11(3):128–131. doi:10.1016/S0955-2863(99)00083-2
    • (2000) J Nutr Biochem , vol.11 , Issue.3 , pp. 128-131
    • Suetsuna, K.1    Ukeda, H.2    Ochi, H.3
  • 24
    • 0006395619 scopus 로고
    • Inhibitory activity against angiotensin I-converting enzyme of peptides originating from fish and shellfish muscle
    • Suetsuna K, Yamagami M, Kuwata K (1988) Inhibitory activity against angiotensin I-converting enzyme of peptides originating from fish and shellfish muscle. Nippon Suisan Gakkaishi 54(10):5
    • (1988) Nippon Suisan Gakkaishi , vol.54 , Issue.10 , pp. 5
    • Suetsuna, K.1    Yamagami, M.2    Kuwata, K.3
  • 25
    • 0034141231 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides
    • COI: 1:CAS:528:DC%2BD3cXhslOqtro%3D
    • Pihlanto-Leppala A, Koskinen P, Piilola K, Tupasela T, Korhonen H (2000) Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Dairy Res 67(1):53–64
    • (2000) J Dairy Res , vol.67 , Issue.1 , pp. 53-64
    • Pihlanto-Leppala, A.1    Koskinen, P.2    Piilola, K.3    Tupasela, T.4    Korhonen, H.5
  • 26
    • 41749086156 scopus 로고    scopus 로고
    • Antihypertensive and antimicrobial bioactive peptides from milk proteins
    • COI: 1:CAS:528:DC%2BD1cXkt1OhtLo%3D
    • Haque E, Chand R (2008) Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur Food Res Technol 227(1):7–15. doi:10.1007/s00217-007-0689-6
    • (2008) Eur Food Res Technol , vol.227 , Issue.1 , pp. 7-15
    • Haque, E.1    Chand, R.2
  • 27
    • 34047162485 scopus 로고    scopus 로고
    • Effect of angiotensin I-converting enzyme inhibitory peptide from rice dregs protein on antihypertensive activity in spontaneously hypertensive rats
    • COI: 1:CAS:528:DC%2BD2sXntVyltr8%3D
    • Chen QH, Xuan GD, Fu ML, He GQ, Wang W, Zhang HB, Ruan H (2007) Effect of angiotensin I-converting enzyme inhibitory peptide from rice dregs protein on antihypertensive activity in spontaneously hypertensive rats. Asia Pac J Clin Nutr 16:281–285
    • (2007) Asia Pac J Clin Nutr , vol.16 , pp. 281-285
    • Chen, Q.H.1    Xuan, G.D.2    Fu, M.L.3    He, G.Q.4    Wang, W.5    Zhang, H.B.6    Ruan, H.7
  • 28
    • 76749118402 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Alaska pollack (Theragra chalcogramma) skin and antioxidant activity of the resulting hydrolysate
    • COI: 1:CAS:528:DC%2BC3cXhvFCksLc%3D
    • Jia J, Zhou Y, Lu J, Chen A, Li Y, Zheng G (2010) Enzymatic hydrolysis of Alaska pollack (Theragra chalcogramma) skin and antioxidant activity of the resulting hydrolysate. J Sci Food Agric 90(4):635–640. doi:10.1002/jsfa.3861
    • (2010) J Sci Food Agric , vol.90 , Issue.4 , pp. 635-640
    • Jia, J.1    Zhou, Y.2    Lu, J.3    Chen, A.4    Li, Y.5    Zheng, G.6
  • 29
    • 4544317465 scopus 로고    scopus 로고
    • Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion
    • COI: 1:CAS:528:DC%2BD2cXnvVOhsro%3D
    • Ruiz JAG, Ramos M, Recio I (2004) Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion. Int Dairy J 14(12):1075–1080. doi:10.1016/j.idairyj.2004.04.007
    • (2004) Int Dairy J , vol.14 , Issue.12 , pp. 1075-1080
    • Ruiz, J.A.G.1    Ramos, M.2    Recio, I.3
  • 30
    • 0034221181 scopus 로고    scopus 로고
    • Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese
    • COI: 1:CAS:528:DC%2BD3cXltVGgt7g%3D
    • Saito T, Nakamura T, Kitazawa H, Kawai Y, Itoh T (2000) Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese. J Dairy Sci 83(7):1434–1440. doi:10.3168/jds.S0022-0302(00)75013-2
    • (2000) J Dairy Sci , vol.83 , Issue.7 , pp. 1434-1440
    • Saito, T.1    Nakamura, T.2    Kitazawa, H.3    Kawai, Y.4    Itoh, T.5
  • 31
    • 33750041097 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin
    • COI: 1:CAS:528:DC%2BD28XhtFSrt77J
    • Yu Y, Hu J, Miyaguchi Y, Bai X, Du Y, Lin B (2006) Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin. Peptides 27(11):2950–2956. doi:10.1016/j.peptides.2006.05.025
    • (2006) Peptides , vol.27 , Issue.11 , pp. 2950-2956
    • Yu, Y.1    Hu, J.2    Miyaguchi, Y.3    Bai, X.4    Du, Y.5    Lin, B.6


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