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The Enzymic Derivation of Citrulline Residues from Arginine Residues In Situ during the Biosynthesis of Hair Proteins that are Cross-Linked by Isopeptide Bonds

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 86A))

Abstract

An enzymic activity present in hair follicles is described that can convert arginine residues to citrulline residues in proteins in situ. The Ca2+ dependent enzyme activity has been detected in hair follicle extracts but not in similar extracts of serum, liver or brain. The enzyme appears to act on proteins other than hair proteins and the citrulline produced can be quantitated in acid hydrolysates by a colorimetric procedure. the formation of citrulline has been confirmed by amino acid analysis and does not appear to be related to the formation of isopeptide linkages which is catalysed by the transamidase present in hair follicles.

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References

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© 1977 Plenum Press, New York

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Rogers, G.E., Taylor, L.D. (1977). The Enzymic Derivation of Citrulline Residues from Arginine Residues In Situ during the Biosynthesis of Hair Proteins that are Cross-Linked by Isopeptide Bonds. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3282-4_17

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  • DOI: https://doi.org/10.1007/978-1-4684-3282-4_17

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3284-8

  • Online ISBN: 978-1-4684-3282-4

  • eBook Packages: Springer Book Archive

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