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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

  • George E. Rogers
  • Lindsay D. Taylor
Part of the Advances in Experimental Medicine and Biology book series (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.

Keywords

Hair Follicle Arginine Residue Root Sheath Protein Citrulline Isopeptide Bond 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • George E. Rogers
    • 1
  • Lindsay D. Taylor
    • 1
  1. 1.Department of BiochemistryUniversity of Adelaide South AustraliaAustralia

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