Superactivity and conformational changes on alpha-chymotrypsin upon interfacial binding to cationic micelles.

@article{Celej2004SuperactivityAC,
  title={Superactivity and conformational changes on alpha-chymotrypsin upon interfacial binding to cationic micelles.},
  author={Mar{\'i}a Soledad Celej and Mariana G D'Andrea and Patricia Targon Campana and Gerardo Daniel Fidelio and Maria Lucia Bianconi},
  journal={The Biochemical journal},
  year={2004},
  volume={378 Pt 3},
  pages={1059-66}
}
The catalytic behaviour of alpha-CT (alpha-chymotrypsin) is affected by cationic micelles of CTABr (hexadecyltrimethylammonium bromide). The enzyme-micelle interaction leads to an increase in both the V(max) and the affinity for the substrate p -nitrophenyl acetate, indicating higher catalytic efficiency for bound alpha-CT. The bell-shaped profile of alpha-CT activity with increasing CTABr concentrations suggests that the micelle-bound enzyme reacts with the free substrate. Although more active… CONTINUE READING

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