Biomedical Engineering Reference
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visible decrease in the fluorescence intensity. The decrease in the intensity is especial
remarkable at 270 nm at a highest content of gelatin in BSA solution (at q=0.4). At the same
time we did not observed any appreciable shift for a position of the maximum of the
fluorescence intensity at any q values.
Figure 6. Antonov et al. “Structural investigation of the interaction between bovine serum albumin and
acid gelatin in water”.
A
GGREGATION OF
BSA
Since the aggregation tendency of BSA upon heating at pH 5.4 (i.e. slightly above the pH
of IEP /4.8-5.0/) depends strongly on its concentration, the effect of the presence of gelatin in
BSA solution was monitored at constant concentration of BSA by the absorbtion of light at
500 nm and DLS measurements. Figure 7. shows the experimental findings in terms of light
adsorbtion.
Figure 7. Antonov et al. “Structural investigation of the interaction between bovine serum albumin and
acid gelatin in water”.
The findings can be interpreted in the following manner: The absorbtion of light of BSA
abd BSA/gelatin solutions decreases as a function of temperature, because of progressing
aggregation. In the binary solutions BSA aggregates as T becomes higher than 56
o
C. The
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