A Rapid Extraction Procedure of Human Hair Proteins and Identification of Phosphorylated Species

January 2002 in “ Biological and Pharmaceutical Bulletin ”

Akira Nakamura, Makoto Arimoto, Keiji Takeuchi, Toshihiro Fujii

human hair proteins thiourea urea reductant hair cortex alpha-keratins matrix proteins SDS-PAGE serine phosphorylation threonine phosphorylation

TLDR A new method quickly extracts and identifies proteins from hair and other keratin sources.

The study developed a rapid extraction procedure for human hair proteins using thiourea and urea with a reductant, effectively isolating proteins from the hair cortex. The extracted proteins included hard alpha-keratins (40-60 kDa), matrix proteins (12-18 kDa), and minor components (110-115 kDa and 125-135 kDa) as identified by SDS-PAGE. Phosphorylation analysis revealed serine phosphorylation in both alpha-keratins and matrix proteins, and threonine phosphorylation in alpha-keratins. The method was also effective for extracting proteins from wool, chicken feathers, rat hair, and human nails.

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research The Catalog of Human Hair Keratins

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research The Catalog of Human Hair Keratins

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Acidic and Basic Hair/Nail (Hard) Keratins: Their Colocalization in Upper Cortical and Cuticle Cells of the Human Hair Follicle and Their Relationship to Soft Keratins

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356 citations , December 1986 in “The journal of cell biology/The Journal of cell biology”

Hair and nail cells share similar proteins, indicating a common differentiation pathway.

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198 citations , October 1986 in “Differentiation”

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32 citations , October 1985 in “Annals of the New York Academy of Sciences”

Keratin genes help explain how hair and feathers develop differently in mammals and birds.