. Biological structure and function; proceedings. Biochemistry; Cytology. 400 550 450 500 Wavelength (m/z) Fig. 13. Difference spectrum (oxidized minus DPNH-trealed), replotted from a tracing obtained with Cary recording spectrophotometer. Negative values denote bleaching. Conditions as in Figs. 11 and 12; soluble extract. E 0-6-. 400 450 500 Fig. 14. Shift of absorption spectrum with pH. rapid (Fig. 12). The difference spectrum resulting from bleaching by the substrate shows minima in the 410 m^a as well as in the flavin region in the initial extract (Fig. 13). In highly purified preparations


. Biological structure and function; proceedings. Biochemistry; Cytology. 400 550 450 500 Wavelength (m/z) Fig. 13. Difference spectrum (oxidized minus DPNH-trealed), replotted from a tracing obtained with Cary recording spectrophotometer. Negative values denote bleaching. Conditions as in Figs. 11 and 12; soluble extract. E 0-6-. 400 450 500 Fig. 14. Shift of absorption spectrum with pH. rapid (Fig. 12). The difference spectrum resulting from bleaching by the substrate shows minima in the 410 m^a as well as in the flavin region in the initial extract (Fig. 13). In highly purified preparations a single broad minimum centring around 425 m/x is observed and the bleaching is more extensive than could be ascribed to the flavin 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 IUB/IUBS International Symposium (1st : 1960 : Stockholm); International Union of Biochemistry; International Union of Biological Sciences; Goodwin, T. W. (Trevor Walworth); Lindberg, Olov, 1914-. London, New York, Academic Press


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