51. Presence of d-amino-acid oxidase protein in mutant mice lacking d-amino-acid oxidase activity
- Author
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Yasumura Yosihiro, Niwa Akira, Yamamoto Katsuhiko, and Konno Ryuichi
- Subjects
D-Amino-Acid Oxidase ,Mutant ,D-amino acid oxidase ,Kidney ,medicine.disease_cause ,Microbodies ,Biochemistry ,Mice ,chemistry.chemical_compound ,Biosynthesis ,medicine ,Animals ,chemistry.chemical_classification ,Oxidase test ,Mutation ,biology ,Peroxisome ,Molecular biology ,Mice, Mutant Strains ,Enzyme ,chemistry ,biology.protein ,Antibody ,Protein Processing, Post-Translational ,Subcellular Fractions - Abstract
1. 1. Mutant mice lacking d -amino-acid oxidase activity were examined as to whether they possessed the enzyme protein. 2. 2. Immunoblotting using an antibody against hog kidney d -amino-acid oxidase showed that kidney homogenates of the mutant mice as well as that of the normal mice had proteins reactive to the antibody. 3. 3. Peroxisomal proteins of the kidney cells of the mutant mice were not different from those of the normal mice. 4. 4. The peroxisomes of the mutant mice possessed a protein reactive to the antibody in the immunoblotting whose size was the same as the d -amino-acid oxidase protein present in the peroxisomes of the normal mice. 5. 5. These results suggest that the mutant mice synthesize the d -amino-acid oxidase protein and integrate it into peroxisomes, though it is a nonfunctional enzyme.
- Published
- 1991