Studies on Isolated Keratin Fractions from Mammalian Epidermis

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Abstract
A protein fraction precipitated at pH 5.5 from an alkaline extract of human epidermis or stratum corneum was not homogeneous on Sephadex gel filtration. The inhomogeneity was due to aggregation phenomena since polyacrylamide gel electrophoresis of all Sephadex fractions gave the same results: a highly-aggregated immobile protein plus two mobile protein bands that represented lower aggregates or subunits. This electrophoretic pattern was found for all the isolated fractions even for fractions with different iso-electrical points (IEP) and from different species. Freshly-ground callus gave essentially the same pattern, indicating that the bands are not artefacts caused by denaturation. The significance for the process of keratinizatíon is discussed.

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