Fatty acyl coupled catalase.
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 greater than 7.0 but became octanol and ether soluble at pH less than 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.
Rosen
G
G
Department of Biochemistry, Hebrew University Medical School, Jerusalem, Israel.
Bar-Tana
J
J
D000215:Acylation; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002374:Catalase / Q000032:analysis / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D003066:Coenzyme A Ligases / Q000378:metabolism; D017886:Durapatite; D006863:Hydrogen-Ion Concentration; D006882:Hydroxyapatites; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D011402:Pronase / Q000378:metabolism; D051381:Rats; D013229:Stearic Acids / Q000378:metabolism*; D014227:Triazines / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D006882:Hydroxyapatites; D013229:Stearic Acids; D014227:Triazines; D017886:Durapatite; D002374:Catalase; D014357:Trypsin; D011402:Pronase; D003066:Coenzyme A Ligases