[Studies on catabolism of ether lipids. -Solubilization of alkylglycerol monooxygenase from rat liver microsome (author's transl)].
The author has investigated the condition for solubilization of alkylglycerol monooxygenase from rat liver microsome. The solubilization of this enzyme has been done by using Triton X-100, because this enzyme is considered to be relatively stable in the presence of 0.5% Triton X-100. It is suggested that there are factors leading to decrement of enzyme activity during the procedure of DEAE-cellulose column chromatography. Since the enzyme activity is markedly stimulated by phosphatidyl choline or catalase in the enzyme system obtained by DEAE-cellulose chromatography, it is presumed that the enzyme activity is markedly reduced because of removing the H2O2-scavenging system as well as the lipids, which are necessary to activate or stabilize the enzyme, from the microsomal enzyme system. Key words: Alkyglycerol monoxygenase, Solubilization, Microsome.
D000818:Animals; D002374:Catalase; D002848:Chromatography, DEAE-Cellulose; D005989:Glycerides; D006861:Hydrogen Peroxide; D066298:In Vitro Techniques; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D006899:Mixed Function Oxygenases; D017830:Octoxynol; D010743:Phospholipids; D011092:Polyethylene Glycols / Q000494:pharmacology; D051381:Rats; D012995:Solubility
D005989:Glycerides; D010743:Phospholipids; D011092:Polyethylene Glycols; D017830:Octoxynol; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; D002374:Catalase; C020678:glyceryl-ether monooxygenase