The incorporation of H3-tyrosine into the protein of the cells in the cortex of rat hair has been investigated by radioautography. In growing hairs, radioactivity is found in the matrix, the upper bulb, and the whole of the keratogenous zone up to the fully keratinized part of the shaft, 10 and 30 minutes after an injection of labelled tyrosine. This is unequivocal evidence of protein synthesis at these sites. There is a very precise relationship between the end of protein synthesis and the hardening of the cortical cells at the top of the keratogenous zone. The way in which the silver grains of the radioautographs are clustered indicates that at 30 minutes after the injection the isotope is distributed more evenly in the matrix and upper bulb than in the top of the keratogenous zone. Possibly this reflects a difference, at these sites, in the cell components engaged in protein synthesis, or in the proteins being synthesized. The fully keratinized and hardened part of the hair was not radioactive at 10 and 30 minutes after the injection of H3-tyrosine. The rate at which the radioactivity moves into this region shows that the hair of rats grows 0.9 mm/24 hours. Comparison of the degree of radioactivity along the growing hair in the 30-minute, 12-hour, and 36-hour materials shows conclusively that protein accumulates in the cortical cells during their keratinization. An injection of a labelled amino acid does not behave as an ideal pulse dose; consequently, the grain density over the hair cortex at 36 hours is 100 per cent larger than would be expected if an ideal pulse dose situation existed.

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