Notes

1. Good correlation was obtained also between activity and AA,em for subtilisin Carlsberg and subtilisin BPN' (1).

2. Fluorescence intensity can be used instead of quantum yield.

200 220 240 260

Wavelength(nm)

Fig. 3. Changes of CD of a-chymotrypsin by changes of solvent composition (w represents water content).

200 220 240 260

Wavelength(nm)

Fig. 3. Changes of CD of a-chymotrypsin by changes of solvent composition (w represents water content).

3. When buffer solutions are used, the salts of buffer components precipitate at high concentrations of organic solvents. In these cases, enzymes form either free suspensions or coprecipitates with salts. Under these conditions, solutions are not buffered, and, therefore, it is advisable to use pure water or buffer solutions of low concentrations (e.g., <0.01 M) to avoid excess turbidity.

4. From X-ray diffraction data, the contents of a-helix and p-sheet structure were determined as 9% and 34%, respectively (8).

5. As stated in the text, CD is basically the difference in absorbance for left- and right-circularly polarized light. Therefore, samples with high absorbance tend to give CD spectra of low reproducibility even if the difference AA is small. It is helpful to measure both CD and absorption spectra for a sample solution.

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