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Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide
Author(s) -
Megan M. Mahoney,
Agnes Y. Lee,
Donna J. Brezinski-Caliguri,
Kenneth Huttner
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01390-3
Subject(s) - peptide , gene , peptide sequence , biology , rna , amino acid , antimicrobial , cleavage (geology) , coding region , sequence analysis , genetics , microbiology and biotechnology , chemistry , biochemistry , paleontology , fracture (geology)
Cathelin‐related genes are characterized by the presence of a prepro sequence which is highly conserved both within and between species. 3′ RACE analysis on sheep bone marrow RNA, using a primer based on a conserved cathelin family coding region, demonstrated the presence of at least three ovine cathelin‐related cDNAs. One of these encodes a novel prepropeptide with a predicted C‐terminal cleavage product RGLRRLGRKIAHGVKKYGPTVLRIIRIAG. The chemically synthesized form of this 29 amino acid peptide is shown to be a thermostable, broad spectrum, bactericidal agent.