Abstract

The “low-sulphur” keratin proteins that comprise the major fibrous protein of hair have been synthesised in a reconstituted cell-free system containing polyribosomes and supernatant factors isolated from guinea pig hair follicle tissue. The evidence for this is precise co-chromatography on Sephadex and co-electrophoresis on acrylamide gels of the radioactively labelled proteins synthesised in vitro with the native proteins extracted from the hair follicle. Further evidence is that the labelled proteins precipitated with antisera prepared against the native hair follicle “low-sulphur” keratin proteins.

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