Protein Modification During Aging of Organism

Authors

  • J. Sajdok Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague ,
  • A. Kozak Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague ,
  • J. Zidkova Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague ,
  • P. Kotrba Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague ,
  • A. Pilin Department of Forensic Medicine, University Hospital, Prague
  • J. Kas Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague ,

Abstract

In the course of aging of organisms, various modifications of side chains of amino acid residues in proteins affect their biological stability and turnover. The main alterations in protein structure are: changes in conformation of proteins, oxidation of amino acid residues (mixed-function oxidation) and racemization of L-amino acids (glutamic and aspartic acids and serine) to corresponding D-forms. D-amino acids were found in bones, teeth, brain and eye lenses. It is generally accepted that the content of D-amino acids slowly increases with age due to a lower metabolic turnover. The discovery of specific D-serine racemase brings a new view of this topic.

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Published

2001-03-15

How to Cite

Sajdok, J., Kozak, A., Zidkova, J., Kotrba, P., Pilin, A., & Kas, J. (2001). Protein Modification During Aging of Organism. Chemické Listy, 95(2). Retrieved from http://ww-w.chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/2444

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