哺乳动物抗菌肽及其在畜牧生产上的应用前景

[1] Amino acid sequence of PR-39: Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Agerberth B,Lee J Y,et al. European Journal of Biochemistry . 1991

[2] Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract. Huttner K M,Brezinski D J,et al. The Journal of Nutrition . 1998

[3] Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Boman H G,Agerberth B,et al. Infection and Immunity . 1993

[4] Membrane thinning effect of the β-sheet antimicrobial protegrins. Hel′er W T,Waring A J,et al. Biochemiwtry . 2000

[5] Epithelial antibiotics induced at sites of inflammation. Schonwetter B S,Stolzeberg E D,et al. Science . 1995

[6] Transcriptional regulation ofβ-defensin gene expression on tracheal epithalial cells. Diamond G,Kaiser V,et al. Infection and Immunity . 2000

[7] Purification and properties of prolinerich antimicrobial peptides from sheep and goat leukocytes. Shamova O,Brogden K A,et al. Infection and Immunity . 1999

[8] Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Christensen B,Fink J,et al. Proceedings of the National Academy of Sciences of the United States of America . 1988

[9] Crystal structure of defensin HNP-3, an amphiphilic dime: mechanisms of membraene permeabilization. Hill C P,Yee J,et al. Science . 1991

[10] Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice. Yarus S,Rosen J M,et al. Proceedings of the National Academy of Sciences of the United States of America . 1996

[1] Amino acid sequence of PR-39: Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Agerberth B,Lee J Y,et al. European Journal of Biochemistry . 1991

[2] Antimicrobial peptide expression is developmentally regulated in the ovine gastrointestinal tract. Huttner K M,Brezinski D J,et al. The Journal of Nutrition . 1998

[3] Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Boman H G,Agerberth B,et al. Infection and Immunity . 1993

[4] Membrane thinning effect of the β-sheet antimicrobial protegrins. Hel′er W T,Waring A J,et al. Biochemiwtry . 2000

[5] Epithelial antibiotics induced at sites of inflammation. Schonwetter B S,Stolzeberg E D,et al. Science . 1995

[6] Transcriptional regulation ofβ-defensin gene expression on tracheal epithalial cells. Diamond G,Kaiser V,et al. Infection and Immunity . 2000

[7] Purification and properties of prolinerich antimicrobial peptides from sheep and goat leukocytes. Shamova O,Brogden K A,et al. Infection and Immunity . 1999

[8] Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Christensen B,Fink J,et al. Proceedings of the National Academy of Sciences of the United States of America . 1988

[9] Crystal structure of defensin HNP-3, an amphiphilic dime: mechanisms of membraene permeabilization. Hill C P,Yee J,et al. Science . 1991

[10] Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice. Yarus S,Rosen J M,et al. Proceedings of the National Academy of Sciences of the United States of America . 1996