Topological location of diamine oxidase in the transverse plane of rabbit liver microsomal membranes.
The transverse topology of diamine oxidase within rabbit liver microsomal membranes was studied by examining the proteolytic digestion of sealed or detergent-permeabilized microsomal vesicles. Trypsin and pronase had no effect on diamine oxidase activity in any incubation conditions tested, while nagarse treatment reduced by 60-70% the enzymic activity of intact microsomes; no further loss of activity was observed in the presence of detergent. These results demonstrate that the active site of diamine oxidase faces the cytoplasmic membrane surface, and suggest that it does not possess or expose on either membrane surfaces bonds susceptible to the proteolytic attack by trypsin or pronase. The possible significance and the biological implications of the results are discussed.
D006631:Amine Oxidase (Copper-Containing) / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D005260:Female; D007425:Intracellular Membranes / Q000201:enzymology; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D017830:Octoxynol; D010447:Peptide Hydrolases / Q000494:pharmacology; D010539:Permeability; D011092:Polyethylene Glycols; D011817:Rabbits
D011092:Polyethylene Glycols; D017830:Octoxynol; D006631:Amine Oxidase (Copper-Containing); D010447:Peptide Hydrolases