The fully differentiated anucleate cells of the stratum corneum of newborn rat epidermis contain a cationic protein called stratum corneum basic protein (SCBP). This protein has a molecular weight (49000) and an amino acid composition similar to a protein extracted from the less differentiated cell layers of the epidermis. Pulse-chase experiments with radiolabeled histidine were undertaken to test the possibility that SCBP is derived from a preexisting protein. A protein of 52 000 daltons is rapidly but transiently labeled in extracts of the less differentiated cell layers. As the amount of label in the 52 000-dalton protein decreases, an increase in radiolabel is observed in extracts of the fully differentiated cells. This label is found in SCBP, a protein of lower molecular weight (49 000) than that initially labeled. These proteins are immunologically related and both are resistant to cyanogen bromide cleavage. They differ in apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gels and in their net charge. The results are consistent with the conversion of a precursor protein into SCBP. © 1979, American Chemical Society. All rights reserved.
