The hydrodynamic properties and kinetic constants with natural substrates of the esterase from Malus pumila fruit.

@article{Goodenough1982TheHP,
  title={The hydrodynamic properties and kinetic constants with natural substrates of the esterase from Malus pumila fruit.},
  author={Peter W. Goodenough and T G Entwistle},
  journal={European journal of biochemistry},
  year={1982},
  volume={127 1},
  pages={145-9}
}
1. An esterase (EC 3.1.1.1) from Malus pumila fruit was purified to homogeneity using ammonium sulphate precipitation, absorption on hydroxyapatite, dye Matrex affinity chromatography, S.300 Sephacryl chromatography and wide-range isoelectric focusing. 2. Kinetic constants of these preparations were established for a series of natural ester substrates. Greatest apparent affinity was for acetate esters containing seven or eight-carbon skeletons and least for four-carbon skeletons. 3. The… CONTINUE READING