Purification and primary structure of murine cryptdin‐1, a Paneth cell defensin

FEBS Letters

Selsted, Michael E.³  Miller, Samuel I.⁴  Ouellette, Andre J.²  Henschen, Agnes H.¹ 

[1] Department of Molecular Biology and Biochemistry, University of California, USA;Cell Biology Unit, Shriners Burns Institute, Surgical, Massachusetts General Hospital and Department of Surgery, Harvard Medical School, Boston, MA 02114, USA;Department of Pathology, University of California School of Medicine, Irvine, CA 92717, USA;Medical Services, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA

关键词: Antimicrobial peptide;    Salmonella;    Cation-exchange chromatography;    High performance liquid chromatography (HPLC);    Peptide sequencing;   

DOI  :  10.1016/0014-5793(92)80606-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have purified and determined the amino acid sequence of cryptdin-1, a murine Paneth cell defensin. The peptide corresponds to a previously characterized mRNA that accumulates to high abundance during postnatal ontogeny of the small bowel. Acid-extracted intestinal protein was fractionated by cation-exchange chromatography and fractions were assayed for antimicrobial activity. One peak of anti-Salmonella activity contained a putative defensin, based on its predicted electrophoretic migration in acid-urea PAGE. The peptide was purified to homogeneity by RP-HPLC and sequenced. These studies demonstrate defensin expression in non-myeloid tissue. The N-terminal extension of cryptdin-1 is a unique structural feature of this novel epithelial defensin.

【 授权许可】

Unknown