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The Journal of Cell Biology, Vol 52, 453-464, Copyright © 1972 by Rockefeller University Press

ARTICLE

FURTHER CHARACTERIZATION OF BOVINE KERATOHYALIN



Arthur R. Ugel 1 and William Idler 1

1 From the Dermatology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014; and the Department of Dermatology, New York University School of Medicine, New York 10016

Extraction of serial sections of cattle hoof epidermis with solutions of calcium chloride, magnesium chloride, potassium chloride, sodium chloride, guanidine hydrochloride, ammonium sulfate, and potassium phosphate buffer (pH 7.0) at varying salt concentrations demonstrates that keratohyalin (KH) is extracted by these salts at certain molarities. Under given conditions of time and temperature, each salt has a specific extraction pattern, and similar salts have similar extraction patterns. Dialysis of the salt extracts of hoof epidermis against distilled water results in the macroaggregition of KH, as assayed by histochemical methods. Although the various macroaggregates appear identical at the histochemical level, they display different ultrastructural characteristics. Polyacrylamide gel electrophoresis of the sodium decyl sulfate-solubilized macroaggregates results in the fractionation of a 20 (or more) member homologous series of oligomers. Isolation of the various oligomeric species of bovine keratohyalin and re-electrophoresis indicate that the various KH species can undergo depolymerization. Amino acid analyses of the unfractionated bovine macroaggregates and the various molecular weight species of bovine KH are similar, further demonstrating homology of the oligomers. The molecular weight of the subunit (monomer) of bovine KH is 14,955, estimated from the amino acid analyses.

Submitted on August 3, 1971
Revised on October 1, 1971


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