Collect. Czech. Chem. Commun.
1991, 56, 712-717
https://doi.org/10.1135/cccc19910712
Trypsin entrapped within liposomes. Partition of a low-molecular-mass substrate as the main factor in kinetic control of hydrolysis
Jana Formelováa, Albert Breiera,*, Peter Gemeinerb and Lubica Kurillováb
a Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, 842 33 Bratislava
b Institute of Chemistry, Slovak Academy of Sciences, 842 38 Bratislava
Abstract
Trypsin has been entrapped within liposomes prepared from egg yolk phospholipides by the method of controlled dialysis, and the hydrolysis kinetics of Nα-benzoyl-DL-arginine p-nitroaniline catalyzed by the liposome-entrapped trypsin has been studied by monitoring the flux of substrate and product across the liposomal membrane. The partitioning of the substrate and product between liposomal and extraliposomal environment has been found to represent the main factor in the kinetic control of the hydrolysis.
