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Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow.

作者信息

Pungercar J, Strukelj B, Kopitar G, Renko M, Lenarcic B, Gubensek F, Turk V

机构信息

Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Ljubljana, Slovenia.

出版信息

FEBS Lett. 1993 Dec 27;336(2):284-8. doi: 10.1016/0014-5793(93)80821-b.

Abstract

Screening of a porcine bone marrow cDNA library with a PCR-derived probe from rabbit LPS-binding protein CAP18 led to the discovery of two closely related clones. The longer, full-length cDNA clone encodes a 228 amino acid residue protein similar to the family of antibacterial/LPS-binding cationic peptides. In contrast to other hitherto discovered precursors of Pro/Arg-rich peptides from this family, they have a novel, unique structure of the C-terminal region of 100 amino acid residues with a repeating sequence of ten residues (FPPPNXPGPR, where X = V or F). These precursors could represent a part of the antibacterial peptide repertoire of porcine bone marrow.

摘要

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