Fatty acyl coupled catalase

Graciela Rosen, Jacob Bar-Tana*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Bovine liver catalase (hydrogen-peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6) was derivatized by 9″(10″)-[4′-{2-(4,6-dichloro-1,3,5-triazinyl)oxy}butoxy]stearic acid and the fatty acyl-coated enzyme was separated from native catalase and excess reagent by hydroxyapatite chromatography. The derivatization of catalase resulted in coupling the long-chain fatty acyl residues to lysine, histidine and arginine, while other amino acids remained essentially unaffected. The fatty acyl-coated enzyme was water soluble at pH > 7.0 but became octanol and ether soluble at pH < 6.5. The derivatized enzyme retained 50-80% of the catalatic- and peroxidative-specific activities. The free carboxyl function of the coupled long-chain fattyl acyl residues could serve as substrate for ATP-dependent CoA-thioesterification catalyzed by the rat liver microsomal long-chain fatty acyl-CoA synthase.

Original languageEnglish
Pages (from-to)264-269
Number of pages6
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume994
Issue number3
DOIs
StatePublished - 23 Feb 1989

Keywords

  • Catalase
  • Fatty acid

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