Elsevier

FEBS Letters

Volume 304, Issues 2–3, 15 June 1992, Pages 146-148
FEBS Letters

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

https://doi.org/10.1016/0014-5793(92)80606-HGet rights and content
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Abstract

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.

Keywords

Antimicrobial peptide
Salmonella
Cation-exchange chromatography
High performance liquid chromatography (HPLC)
Peptide sequencing

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