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Pepsin difference spectra

In Fig. 3, the pepsin dissolved in HC1, without interaction with any solid, showed a maximum at 272 nm. After interaction with the disordered cancrinite and the intermediate phase, a small decrease in the absorbance maximum of the pepsin spectrum was observed. This small decrease is due to the pepsin adsorption on the solid surfaces. The pepsin activity was also determined by the proteolysis reaction of a denatured haemoglobin solution at different times. Fig. 4 shows the obtained results. One can see, that the enzymatic activities (determined as absorbance), presented by the tested solids were very similar among them. These results show that pepsin enzymatic activity is not lost after the contact the pepsin with the tested solids. Therefore, the absorbance decrease observed in Fig. 4, is produced by the pepsin adsorption on the tectosilicate surface, and not by chemical reactions between pepsin and the tectosilicates... [Pg.148]


See other pages where Pepsin difference spectra is mentioned: [Pg.355]    [Pg.373]    [Pg.89]    [Pg.99]    [Pg.360]    [Pg.501]    [Pg.286]    [Pg.368]    [Pg.45]   
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