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• W2090102372 abstract "1. The spectral properties of soluble complexes of chymotrypsinogen A with the polyanions, DNA or soluble carboxymethylcellulose, and the effects of heating on these properties and on the integrity of the DNA complex have been studied. The extrapolation method1 has been found reliable for correcting the observed spectra for light scattering. 2. Complex formation per se between chymotrypsinogen and either DNA or carboxymethylcellulose has little or no effect on the true absorbance (240–300 mμ) of the two components. This implies that no significant conformational change, detectable by spectral measurements, is induced in either component. 3. Although coagulation of the protein does not occur when chymotrypsinogen complexes with polyanions are heated, denaturation of the protein, as measured by spectral changes, is not prevented by complex formation. In fact, complex formation results in an increased rate of protein denaturation (see also Hofstee2). 4. As shown by ultracentrifugation, as heating of the chymotrypsinogen-DNA complex progresses from 25° to 60°, release of the protein gradually occurs in a temperature range from about 40° to 55°. The release of the protein occurs concomitantly with absorbance changes (e.g. at 292 mμ), implying a close correlation between denaturation and release from DNA binding. The decrease in light scattering (measured at 340 mμ) of the complex during heating provides a convenient means of following the dissociation of the complexes. 5. Under the conditions employed, a temperature separation of the absorbance changes of the DNA and the chymotrypsinogen components appears to have been achieved, protein changes occurring prior to and DNA changes occurring after 60°. 6. The results imply a separation of the protein denaturation process into two phases, the absorbance changes at 240 mμ and 292 mμ occurring prior to those at 260 mμ. 7. Evidence is presented that heat coagulation of chymotrypsinogen per se is initiated by complex formation between native and denatured molecules rather than through self-aggregation of the denatured products. The presence of the polyanions, which bind the positively-charged native configuration, would prevent association of the native protein with the unbound negatively-charged denatured product." @default.
• W2090102372 created "2016-06-24" @default.
• W2090102372 creator A5009626787 @default.
• W2090102372 date "1968-02-01" @default.
• W2090102372 modified "2023-09-25" @default.
• W2090102372 title "Spectral properties of chymotrypsinogen-DNA complexes and the effects of heating" @default.
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• W2090102372 doi "https://doi.org/10.1016/0005-2787(68)90200-1" @default.
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