Premium
New caerin 1 antibiotic peptides from the skin secretion of the Australian tree frog Litoria chloris . Part 2. Sequence determination using electrospray mass spectrometry
Author(s) -
Wabnitz Paul A.,
Steinborner Simon T.,
Currie Graeme J.,
Bowie John H.,
Tyler Michael J.
Publication year - 1998
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19980131)12:2<53::aid-rcm115>3.0.co;2-b
Subject(s) - chemistry , edman degradation , electrospray mass spectrometry , electrospray , mass spectrometry , tree frog , chromatography , peptide , peptide sequence , stereochemistry , biochemistry , biology , gene , ecology
Electrospray mass spectrometry and automated Edman sequencing provides the structures of two new caerin 1 antimicrobial peptides from the skin glands of the Australian tree frog Litoria chloris. These are: caerin 1.8 Gly Leu Phe Lys Val Leu Gly Ser Val Ala Lys His Leu Leu Pro His Val Val Pro Val Ile Ala Glu Lys Leu (NH 2 ), and caerin 1.9, Gly Leu Phe Gly Val Leu Gly Ser Ile Ala Lys His Val Leu Pro His Val Val Pro Val Ile Ala Glu Lys Leu (NH 2 ). © 1998 John Wiley & Sons, Ltd.