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Volumn 65, Issue 1, 2009, Pages 23-29

Cloning, expression, isotope labeling, purification, and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli

Author keywords

Antimicrobial peptide; Bovine lactophorin; Expression; Lactophoricin; Membrane protein; Solid state NMR studies; Solution NMR studies

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; HYBRID PROTEIN; MILK PROTEIN;

EID: 60349118324     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.12.009     Document Type: Article
Times cited : (41)

References (28)
  • 1
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E.W. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1 (2001) 156-164
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.W.1
  • 2
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E.W., and Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24 (2006) 1551-1577
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1577
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 4
    • 0345511905 scopus 로고    scopus 로고
    • Ovine antimicrobial peptides: new products from an age-old industry
    • Anderson R.C., Wilkinson B., and Yu P.L. Ovine antimicrobial peptides: new products from an age-old industry. Aust. J. Agr. Res. 55 (2004) 69-75
    • (2004) Aust. J. Agr. Res. , vol.55 , pp. 69-75
    • Anderson, R.C.1    Wilkinson, B.2    Yu, P.L.3
  • 5
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • Heilbom J.D., Nilsson M.F., Kratz G., Weber G., Sǿrensen O., Borregaard N., and Ståhle-Bäckdahl M. The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J. Invest. Dermatol. 120 (2003) 379-389
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 379-389
    • Heilbom, J.D.1    Nilsson, M.F.2    Kratz, G.3    Weber, G.4    Sø ́rensen, O.5    Borregaard, N.6    Ståhle-Bäckdahl, M.7
  • 7
    • 18044397724 scopus 로고    scopus 로고
    • Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines
    • Mader J.S., Salsman J., Conrad D.M., and Hoskin D.W. Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol. Cancer Ther. 4 (2005) 612-624
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 612-624
    • Mader, J.S.1    Salsman, J.2    Conrad, D.M.3    Hoskin, D.W.4
  • 12
    • 0347755460 scopus 로고    scopus 로고
    • APD: the antimicrobial peptide database
    • Wang Z., and Wang G.S. APD: the antimicrobial peptide database. Nucleic Acids Res. 32 (2004) D590-D592
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.S.2
  • 13
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 3 (2005) 247-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 247-250
    • Brogden, K.A.1
  • 14
    • 1542315480 scopus 로고    scopus 로고
    • In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin
    • Saido-Sakanaka H., Ishibashi J., Momotani E., Amano F., and Yamakawa M. In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin. Peptides 25 (2004) 19-27
    • (2004) Peptides , vol.25 , pp. 19-27
    • Saido-Sakanaka, H.1    Ishibashi, J.2    Momotani, E.3    Amano, F.4    Yamakawa, M.5
  • 15
    • 2942592590 scopus 로고    scopus 로고
    • Inactivation of virus infecting ectothermic animals by amphibian and piscine antimicrobial peptides
    • Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D., and Rollins-Smith L. Inactivation of virus infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology 323 (2004) 268-275
    • (2004) Virology , vol.323 , pp. 268-275
    • Chinchar, V.G.1    Bryan, L.2    Silphadaung, U.3    Noga, E.4    Wade, D.5    Rollins-Smith, L.6
  • 16
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock R.E.W. Peptide antibiotics. Lancet 349 (1997) 418-422
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 17
    • 0004280724 scopus 로고
    • Revue bibliographique: la fraction protéose-peptones du lait
    • Pâquet D. Revue bibliographique: la fraction protéose-peptones du lait. Le Lait 69 (1989) 1-21
    • (1989) Le Lait , vol.69 , pp. 1-21
    • Pâquet, D.1
  • 18
    • 0023355583 scopus 로고
    • Characterization of a heterogeneous camel milk whey non-casein protein
    • Beg O.U., von Bahr-Lindström H., Zaidi Z.H., and Jörnvall H. Characterization of a heterogeneous camel milk whey non-casein protein. FEBS Lett. 216 (1987) 270-274
    • (1987) FEBS Lett. , vol.216 , pp. 270-274
    • Beg, O.U.1    von Bahr-Lindström, H.2    Zaidi, Z.H.3    Jörnvall, H.4
  • 19
    • 0025108033 scopus 로고
    • Direct identification and characterization of llama (Lama glama L.) whey proteins by microsequencing after western blotting
    • Cantisani A., Napolitano L., Giuffrida M.G., and Conti A. Direct identification and characterization of llama (Lama glama L.) whey proteins by microsequencing after western blotting. J. Biochem. Biophys. Methods 21 (1990) 227-236
    • (1990) J. Biochem. Biophys. Methods , vol.21 , pp. 227-236
    • Cantisani, A.1    Napolitano, L.2    Giuffrida, M.G.3    Conti, A.4
  • 20
    • 0031308826 scopus 로고    scopus 로고
    • The localization and multimeric nature of component PP3 in bovine milk: purification and characterization of PP3 from caprine and ovine milks
    • Sørensen E.S., Rasmussen L.K., Møller L., and Petersen T.E. The localization and multimeric nature of component PP3 in bovine milk: purification and characterization of PP3 from caprine and ovine milks. J. Dairy Sci. 80 (1997) 3176-3181
    • (1997) J. Dairy Sci. , vol.80 , pp. 3176-3181
    • Sørensen, E.S.1    Rasmussen, L.K.2    Møller, L.3    Petersen, T.E.4
  • 21
    • 0032134034 scopus 로고    scopus 로고
    • The primary structure of caprine PP3: amino acid sequence, phosphorylation, and glycosylation of component PP3 from the proteose-peptone fraction of caprine milk
    • Lister I.M., Rasmussen L.K., Johnsen L.B., Møller L., Petersen T.E., and Sørensen E.S. The primary structure of caprine PP3: amino acid sequence, phosphorylation, and glycosylation of component PP3 from the proteose-peptone fraction of caprine milk. J. Dairy Res. 81 (1998) 2111-2115
    • (1998) J. Dairy Res. , vol.81 , pp. 2111-2115
    • Lister, I.M.1    Rasmussen, L.K.2    Johnsen, L.B.3    Møller, L.4    Petersen, T.E.5    Sørensen, E.S.6
  • 22
    • 3142527103 scopus 로고    scopus 로고
    • Antibacterial activity of Lactophoricin, a synthetic 23-residues peptide derived from the seqeunce of bovine milk component-3 of proteose peptone
    • Campagna S., Mathot A.G., Fleury Y., Dirardet J.M., and Gaillard J.L. Antibacterial activity of Lactophoricin, a synthetic 23-residues peptide derived from the seqeunce of bovine milk component-3 of proteose peptone. J. Dairy Sci. 87 (2004) 1621-1626
    • (2004) J. Dairy Sci. , vol.87 , pp. 1621-1626
    • Campagna, S.1    Mathot, A.G.2    Fleury, Y.3    Dirardet, J.M.4    Gaillard, J.L.5
  • 24
    • 0033049369 scopus 로고    scopus 로고
    • Specific interaction between anionic phospholipids and milk bovine component PP3 and its 119-135 C-terminal fragment
    • Campagna S., Van Mau N., Heitz F., Humbert G., and Gaillard J.L. Specific interaction between anionic phospholipids and milk bovine component PP3 and its 119-135 C-terminal fragment. Colloids Surf. B 13 (1999) 299-309
    • (1999) Colloids Surf. B , vol.13 , pp. 299-309
    • Campagna, S.1    Van Mau, N.2    Heitz, F.3    Humbert, G.4    Gaillard, J.L.5
  • 25
    • 0032238495 scopus 로고    scopus 로고
    • Conformational studies of a synthetic peptide from the putative lipid-binding domain of bovine milk component PP3
    • Campagna S., Vitoux B., Humbert G., Girardet J.M., Linden G., Haertle T., and Gaillard J.L. Conformational studies of a synthetic peptide from the putative lipid-binding domain of bovine milk component PP3. J. Dairy Sci. 81 (1998) 3139-3148
    • (1998) J. Dairy Sci. , vol.81 , pp. 3139-3148
    • Campagna, S.1    Vitoux, B.2    Humbert, G.3    Girardet, J.M.4    Linden, G.5    Haertle, T.6    Gaillard, J.L.7
  • 26
  • 27
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • Kuliopulos A., and Walsh C.T. Production, purification, and cleavage of tandem repeats of recombinant peptides. J. Am. Chem. Soc. 116 (1994) 4599-4607
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 28
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.