. Biological structure and function; proceedings. Biochemistry; Cytology. FUNCTION OF FLAVOENZYMES IN ELECTRON TRANSPORT TABLE IV Properties of Diaphorase Activities of Submitochondrial Fractions Prepared According to Kielley and Kielley (1953) F"or experimental details, see Danielson, F>nster and Ljunggren [25]. 145 Submitochondrial fraction Additions Diaphorase activity /Ltmoles DCPIP reduced/ liver DPNH TPNH Supernatant none 028 030 8 mg. Tween 0-70 071 8 mg. Tween + lo^** M dicoumarol 005 0-04 Pellet (light) none 050 o-oo8 8 mg. Tween 050 0-038 8 mg. Tween + lo""
. Biological structure and function; proceedings. Biochemistry; Cytology. FUNCTION OF FLAVOENZYMES IN ELECTRON TRANSPORT TABLE IV Properties of Diaphorase Activities of Submitochondrial Fractions Prepared According to Kielley and Kielley (1953) F"or experimental details, see Danielson, F>nster and Ljunggren [25]. 145 Submitochondrial fraction Additions Diaphorase activity /Ltmoles DCPIP reduced/ liver DPNH TPNH Supernatant none 028 030 8 mg. Tween 0-70 071 8 mg. Tween + lo^** M dicoumarol 005 0-04 Pellet (light) none 050 o-oo8 8 mg. Tween 050 0-038 8 mg. Tween + lo"" M dicoumarol 0-46 o-oo6 The light sediment exhibited a DPXH oxidase activity, as shown in Table V. This was sensitive to amvtal and antimvcin A. When cytochrome c was added, the respiration was increased, and the stimulated respiration was only partially inhibited by these agents. Thus this pellet seems to. 7 6 5 4 -log M dicoumarol Fig. 3. Effect of dicoumarol on diaphorase activities of submitochondrial fractions prepared according to Kielley and Kielley (1953). Activities measured bv using DPNH as substrate and DCPIP as hydrogen acceptor. For experimental details, see Danielson, Ernster, and Ljunggren [25]. contain both the "internal" type of DPXH oxidase of mitochondria, and the "external" type of DPXH cytochrome c reductase (cf. [26, 27]). As Professor Lindberg reported earlier in this session [28], the two systems may also be distinguished by their different degrees of sensitixitv to desa- minothyroxine. Using the "internal" DPXH oxidase system, that is, the light pellet without supplementation with cytochrome r, it was found that the amytal- block now could not be by-passed by added \ itamin K3 (Fig. 4). However, VOL. II.—L. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original work
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