Premium
Peroxidation of microsomal membrane protein—Lipid complexes
Author(s) -
Victoria Edward J.,
Barber Albert A.
Publication year - 1969
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02531045
Subject(s) - lipid peroxidation , micelle , chemistry , microsome , phospholipid , microsoma , biochemistry , membrane , chromatography , antioxidant , organic chemistry , enzyme , aqueous solution
Nonenzymatic lipid peroxidation was studied using the TBA test on rat liver microsomal fractions, lipid micelles and structural protein‐lipid micelle complexes. The kinetics, response to divalent cations, and iron‐ascorbate catalysis were alike in the microsomal fraction and in the complex, but different in lipid micelles. The structural protein represented 41% of the total membrane protein, had a S 20,obs of 3.5 and was hydrophobic. The binding of lipid micelles by structural protein proceeded in two steps, with an initial fast rate followed by a slower rate. The binding appeared to involve a hyrophobic association between lipid and protein as evidenced by insensitivity to pH, ionic strength and lack of preference for the individual classes of phospholipid micelles. Deoxycholate caused an increase in the initial peroxidation rate in microsomal fractions. Iron and ascorbate catalyzed lipid peroxidation in both the microsomal fraction and in the complex. Iron catalyzed lipid peroxidation but calcium, cobalt and copper inhibited the reaction in the SP‐lipid micelle complex. Lipid peroxidation in microsomal suspensions, therefore, appears to be determined, in part, by the hydrophobic nature of the protein‐lipid association found in membranes.