Partial resolution of the enzymes catalyzing oxidative phosphorylation. X. Correlation of morphology and function in submitochondrial particles.
نویسندگان
چکیده
1. Evidence has been presented in this paper which greatly strengthens the suggestion that the spherical particles lining the inner membranes of mitochondria are the morphological representations of coupling factor 1 (ATPase). 2. With tritum-labeled ATPase it was shown that treatment of reconstituted particles with 2 M urea leads to a release of radioactivity which corresponded to the disappearance of the inner membrane spheres. 3. Certain salts, e.g. KI or KSCN were shown to facilitate the cold inactivation of ATPase in mitochondrial particles and to eliminate the inner membrane spheres. 4. Studies of the structural properties of reconstituted preparations of oligomycin-sensitive ATPase revealed characteristic fragments of membranes with inner membrane spheres. These preparations were essentially colorless and contained negligible amounts of respiratory enzymes. 5. A role of phospholipids in the organization of the membranous fragments was demonstrated.
منابع مشابه
Partial resolution of the enzymes catalyzing oxidative phosphorylation. VII. Oxidative phosphorylation in the diphosphopyridine nucleotide-cytochrome b segment of the respiratory chain: assay and properties in submitochondrial particles.
1. A spectrophotometric procedure is described which specifically measures oxidative phosphorylation in submitochondrial particles in the diphosphopyridine nucleotide-cytochrome b segment of the respiratory chain. It is based on the reduction of exogenous coenzyme Q1 by reduced diphosphopyridine nucleotide catalyzed by phosphorylating submitochondrial particles from beef heart and rat liver. 2....
متن کاملPartial resolution of the enzymes catalyzing oxidative phosphorylation. XXIV. A factor required for the binding of mitochondrial adenosine triphosphatase to the inner mitochondrial membrane.
1. Submitochondrial particles have been sequentially treated with trypsin, mea, and sonic oscillation at an alkaline PH. These TUA particles required addition of a protein (F,,) in order to render added ATPase (Fr) sensitive to dicyclohexylcarbodiimide. Further resolution was obtained by exposure of TUA particles either to 2 M sodium thiocyanate or to 1.5% silicotungstate. These procedures remo...
متن کاملPartial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation VII. OXIDATIVE PHOSPHORYLATION IN THE DIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME b SEGMENT OF THE RESPIRATORY CHAIN: ASSAY AND PROPERTIES IN SUBMITOCHONDRIAL
1. A spectrophotometric procedure is described which specifically measures oxidative phosphorylation in submitochondrial particles in the diphosphopyridine nucleotide-cytochrome b segment of the respiratory chain. It is based on the reduction of exogenous coenzyme Q1 by reduced diphosphopyridine nucleotide catalyzed by phosphorylating submitochondrial particles from beef heart and rat liver. 2....
متن کاملPartial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation. Iii. a New Coupling Factor Required by Submitochondrial Particles Extracted with Phosphatides.
1. The reaction of mitochondrial adenosine triphosphatase (coupling factor 1) with iodine resulted in rapid loss of ATPase activity, disappearance of sulfhydryl groups, binding of iodine to the protein, and partial dissociation of the molecule. The extent of the changes observed depended on the molar ratio of iodine to protein in the reaction mixture. At a molar ratio of 50, more than 99% of th...
متن کاملPartial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
1. Passage of submitochondrial particles through a Sephadex cc,lumn activated the adenosine triphosphatase activity 5to IO-fold and subsequent treatment with urea removed virtually all ATPase (coupling factor 1). The resulting submitochondrial particles, exposed sequentially to Sephadex and urea (SU-particles), catalyzed the oxidation of succinate but phosphorylation was insignificant. P: 0 rat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 241 10 شماره
صفحات -
تاریخ انتشار 1966