Abstract
Protein (HRP), rich in histidine and soluble in o.I.N HCIO 4 at room temperature, has been obtained from keratohyalin granules (KHG) isolated from the epidermis of the newborn rat by extraction with 1M phosphate, pH 7.0, followed by dialysis against H 2 O. HRP constituted about 50 percent of the protein in the isolated KHG which were shown to have staining properties and ultrastructure similar to the in situ KHG. HRP was also obtained from the residual tissue after removal of the KHG. Polyacrylamide disc gel electrophoresis in sodium dodecyl sulfate resolved the total protein of the KHG into 15 separate bands having molecular weights from 12,700 to 93, 000 daltons with highest concentrations of protein at 48,500 and 79,000 daltons. Histidine, aspartic acid, glutamic acid, arginine, serine, threonine, glycine, and alanine constituted 85 percent of the total protein in the KHG. Neither methionine nor cysteine residues were detected. The demonstrated presence of HRP in the KHG makes it possible to investigate molecular phenomena of control in epidermal differentiation.
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