메뉴 건너뛰기




Volumn 232, Issue 4, 2011, Pages 637-646

α 67-106 of bovine hemoglobin: A new family of antimicrobial and angiotensin I-converting enzyme inhibitory peptides

Author keywords

ACE inhibitory activity; Antimicrobial peptides; Bovine hemoglobin; Hydrolysis

Indexed keywords

ESCHERICHIA COLI; HEMOGLOBIN; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; MAMMALS;

EID: 79952987884     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-011-1430-z     Document Type: Article
Times cited : (62)

References (34)
  • 1
    • 0030598623 scopus 로고    scopus 로고
    • Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides derived from hemoglobin
    • Mito K, Fujii M, Kuwahara M, Matsumura N, Shimizu T, Sugano S, Karaki H (1996) Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides derived from hemoglobin. Eur J Pharmacol 304: 93-98.
    • (1996) Eur J Pharmacol , vol.304 , pp. 93-98
    • Mito, K.1    Fujii, M.2    Kuwahara, M.3    Matsumura, N.4    Shimizu, T.5    Sugano, S.6    Karaki, H.7
  • 5
    • 33750041097 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin
    • 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: 2950-2956.
    • (2006) Peptides , vol.27 , pp. 2950-2956
    • Yu, Y.1    Hu, J.2    Miyaguchi, Y.3    Bai, X.4    Du, Y.5    Lin, B.6
  • 7
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55: 27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 8
    • 43049107998 scopus 로고    scopus 로고
    • The antihypertensive effect of peptides: a novel alternative to drugs?
    • Hong F, Ming L, Yi S, Zhanxia L, Yongquan W, Chi L (2008) The antihypertensive effect of peptides: a novel alternative to drugs? Peptides 29: 1062-1071.
    • (2008) Peptides , vol.29 , pp. 1062-1071
    • Hong, F.1    Ming, L.2    Yi, S.3    Zhanxia, L.4    Yongquan, W.5    Chi, L.6
  • 9
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen PM, Peterson D, Dambmann C (2001) Improved method for determining food protein degree of hydrolysis. J Food Sci 66: 642-646.
    • (2001) J Food Sci , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Peterson, D.2    Dambmann, C.3
  • 10
    • 0029744058 scopus 로고    scopus 로고
    • Peptic peptide mapping by HPLC, on line with photodiode array detection, of a haemoglobin hydrolysate produced at pilot-plant scale from an ultrafiltration process
    • Zhao QY, Piot JM, Gautier V, Cottenceau G (1996) Peptic peptide mapping by HPLC, on line with photodiode array detection, of a haemoglobin hydrolysate produced at pilot-plant scale from an ultrafiltration process. Appl Microbiol Biotechnol 45: 778-784.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 778-784
    • Zhao, Q.Y.1    Piot, J.M.2    Gautier, V.3    Cottenceau, G.4
  • 12
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting-enzyme inhibitors from sour milk
    • Nakamura Y, Yamamoto N, Sakai K, Okubo A, Yamazaki S, Takano T (1995) Purification and characterization of angiotensin I-converting-enzyme inhibitors from sour milk. J Dairy Sci 78: 777-783.
    • (1995) J Dairy Sci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 13
    • 0029956552 scopus 로고    scopus 로고
    • Antibacterial activity of glycosylated and phosphorylated chromogranin α-derived peptide 173-194 from bovine adrenal medullary chromaffin granules
    • Strub JM, Goumon Y, Lugardon K, Capon C, Lopez M, Moniatte M, van Dorsselaer A, Aunis D, Metz-Boutigue MH (1996) Antibacterial activity of glycosylated and phosphorylated chromogranin α-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. J Biol Chem 271: 28533-28540.
    • (1996) J Biol Chem , vol.271 , pp. 28533-28540
    • Strub, J.M.1    Goumon, Y.2    Lugardon, K.3    Capon, C.4    Lopez, M.5    Moniatte, M.6    van Dorsselaer, A.7    Aunis, D.8    Metz-Boutigue, M.H.9
  • 14
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe M, Schumann M, Wieprecht T, Winkler A, Beyermann M, Krause E, Matsuzaki K, Murase O, Bienert M (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35: 12612-12620.
    • (1996) Biochemistry , vol.35 , pp. 12612-12620
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 15
    • 0000130569 scopus 로고
    • Multiple and multiple F test
    • Duncan DB (1955) Multiple and multiple F test. Biometrics 11: 1-42.
    • (1955) Biometrics , vol.11 , pp. 1-42
    • Duncan, D.B.1
  • 16
    • 0034117422 scopus 로고    scopus 로고
    • Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases
    • Kristinsson HG, Rasco BA (2000) Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agric Food Chem 48: 657-666.
    • (2000) J Agric Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 17
    • 34547580178 scopus 로고    scopus 로고
    • Time-dependent nature in peptic hydrolysis of native bovine hemoglobin
    • Su RX, Qi W, He ZM (2007) Time-dependent nature in peptic hydrolysis of native bovine hemoglobin. Eur Food Res Technol 225: 637-647.
    • (2007) Eur Food Res Technol , vol.225 , pp. 637-647
    • Su, R.X.1    Qi, W.2    He, Z.M.3
  • 18
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and bacterial activity
    • Powers JPS, Hancock REW (2003) The relationship between peptide structure and bacterial activity. Peptides 24: 1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.S.1    Hancock, R.E.W.2
  • 19
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock RE, Rozek A (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol Lett 206: 143-149.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 143-149
    • Hancock, R.E.1    Rozek, A.2
  • 20
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 21
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 22
    • 33846397753 scopus 로고    scopus 로고
    • In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin s4 derivatives
    • Marynka KS, Rotem I, Portnaya U, Cogan Mor A (2007) In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin s4 derivatives. Chem Biol 14: 75-85.
    • (2007) Chem Biol , vol.14 , pp. 75-85
    • Marynka, K.S.1    Rotem, I.2    Portnaya, U.3    Cogan Mor, A.4
  • 23
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu M, Maier E, Benz R, Hancock RE (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38: 7235-7242.
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 24
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: an overview
    • Andreu D, Rivas L (1998) Animal antimicrobial peptides: an overview. Biopolymers 47: 415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 25
    • 0025962890 scopus 로고
    • Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis
    • Nishikata MT, Kanehira H, Oh H, Tani M, Tazaki Kuboki Y (1991) Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis. Biochem Biophys Res Commun 174: 625-663.
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 625-663
    • Nishikata, M.T.1    Kanehira, H.2    Oh, H.3    Tani, M.4    Tazaki Kuboki, Y.5
  • 26
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel H (1997) Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 43: 119-128.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 27
    • 0035136393 scopus 로고    scopus 로고
    • Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats
    • Wu J, Ding X (2001) Hypotensive and physiological effect of angiotensin converting enzyme inhibitory peptides derived from soy protein on spontaneously hypertensive rats. J Agric Food Chem 49: 501-506.
    • (2001) J Agric Food Chem , vol.49 , pp. 501-506
    • Wu, J.1    Ding, X.2
  • 28
    • 33244488716 scopus 로고    scopus 로고
    • Structural requirements of angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides
    • Wu J, Aluko RE, Nakai S (2006) Structural requirements of angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides. J Agric Food Chem 54: 732-738.
    • (2006) J Agric Food Chem , vol.54 , pp. 732-738
    • Wu, J.1    Aluko, R.E.2    Nakai, S.3
  • 29
    • 67349231325 scopus 로고    scopus 로고
    • A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate
    • Zhao Y, Li B, Dong S, Liu Z, Zhao X, Wang J, Zeng M (2009) A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate. Peptides 30: 1028-1033.
    • (2009) Peptides , vol.30 , pp. 1028-1033
    • Zhao, Y.1    Li, B.2    Dong, S.3    Liu, Z.4    Zhao, X.5    Wang, J.6    Zeng, M.7
  • 30
    • 77949802114 scopus 로고    scopus 로고
    • Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of Cuttlefish (Sepia officinalis) muscle proteins
    • Balti R, Nedjar-Arroume N, Adjé YE, Guillochon D, Nasri M (2010) Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of Cuttlefish (Sepia officinalis) muscle proteins. J Agric Food Chem 58: 3840-3846.
    • (2010) J Agric Food Chem , vol.58 , pp. 3840-3846
    • Balti, R.1    Nedjar-Arroume, N.2    Adjé, Y.E.3    Guillochon, D.4    Nasri, M.5
  • 31
    • 77953637834 scopus 로고    scopus 로고
    • Isolation of an antihypertensive peptide from alcalase digest of Spirulina platensis
    • Lu J, Ren DF, Xue YL, Sawano Y, Miyakawa T, Tanokura M (2010) Isolation of an antihypertensive peptide from alcalase digest of Spirulina platensis. J Agric Food Chem 58: 7166-7171.
    • (2010) J Agric Food Chem , vol.58 , pp. 7166-7171
    • Lu, J.1    Ren, D.F.2    Xue, Y.L.3    Sawano, Y.4    Miyakawa, T.5    Tanokura, M.6
  • 32
    • 77955576619 scopus 로고    scopus 로고
    • Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats
    • Cao W, Zhang C, Hong P, Ji H, Hao J (2010) Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats. Int J Food Sci Technol 45: 959-965.
    • (2010) Int J Food Sci Technol , vol.45 , pp. 959-965
    • Cao, W.1    Zhang, C.2    Hong, P.3    Ji, H.4    Hao, J.5
  • 33
    • 77953135393 scopus 로고    scopus 로고
    • Three novel angiotensin I converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases
    • Balti R, Nedjar-Arroume N, Bougatef A, Guillochon D, Nasri M (2010) Three novel angiotensin I converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Res Int 43: 1136-1143.
    • (2010) Food Res Int , vol.43 , pp. 1136-1143
    • Balti, R.1    Nedjar-Arroume, N.2    Bougatef, A.3    Guillochon, D.4    Nasri, M.5
  • 34
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang Z, Wang G (2004) APD: The antimicrobial peptide database. Nucleic Acids Res 32: D590-D592.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.