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Biochem Biophys Res Commun. 1990 Nov 30;173(1):92-8.

A novel epidermal cell differentiation inhibitor (EDIN): purification and characterization from Staphylococcus aureus.

Author information

1
Department of Microbiology, Hiroshima University School of Dentistry, Japan.

Abstract

A factor inhibiting the calcium-induced terminal differentiation of cultured mouse keratinocytes was purified to homogeneity from the extracellular products of S. aureus E-1 and designated 'epidermal cell differentiation inhibitor' (EDIN). EDIN activity was sensitive to trypsin and heat-labile, suggesting that EDIN is a protein. EDIN gave a single band with a molecular weight of 27,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was found to be a single chain polypeptide, having an isoelectric point higher than 9. The N-terminal amino acid sequence of EDIN was determined as A-D-V-K-N-F-T-D-L. EDIN inhibited the differentiation of not only mouse but also human keratinocytes in culture.

PMID:
2256941
DOI:
10.1016/s0006-291x(05)81026-5
[Indexed for MEDLINE]

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