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. 1987 May;68(2):366–374.

Isolation and purification of ILS, an interleukin 1 inhibitor produced by human gingival epithelial cells.

L J Walsh 1, P E Lander 1, G J Seymour 1, R N Powell 1
PMCID: PMC1542721  PMID: 3498574

Abstract

Recent studies have described the presence of an interleukin 1 (IL-1) inhibitor (ILS) in supernatants from human gingival organ cultures. This report describes the isolation and purification of ILS. ILS was produced in serum-free medium and purified to apparent homogeneity by ion exchange chromatography and high pressure liquid chromatography. IL-1 and ILS eluted as discrete proteins using this system, with ILS appearing as a single protein band of 97,400 molecular weight on SDS-PAGE. ILS inhibited the effects of both murine IL-1 and IL-2 on thymocyte proliferation, and was heat resistant, moderately resistant to freeze-thawing and stable for 2 years at 0-4 degrees C or -20 degrees C. Production of ILS by gingival epithelial cell cultures was not affected by depletion of Langerhans cells, implying that ILS is primarily a keratinocyte product.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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