Trypsin entrapped within liposomes. Partition of a low-molecular-mass substrate as the main factor in kinetic control of hydrolysis

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Title:Trypsin entrapped within liposomes. Partition of a low-molecular-mass substrate as the main factor in kinetic control of hydrolysis
Creators:
Formelová, Jana
Breier, Albert
Gemeiner, Peter
Kurillová, Lubica
Journal or Publication Title:
Collection of Czechoslovak Chemical Communications, 56, 3, pp. 712-717

Abstract

Trypsin has been entrapped within liposomes prepared from egg yolk phospholipides by the method of controlled dialysis, and the hydrolysis kinetics of N<sup>α</sup>-benzoyl-DL-arginine <i>p</i>-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.

Title:Trypsin entrapped within liposomes. Partition of a low-molecular-mass substrate as the main factor in kinetic control of hydrolysis
Creators:
Formelová, Jana
Breier, Albert
Gemeiner, Peter
Kurillová, Lubica
Divisions:Life and Chemical Sciences > Institute of Organic Chemistry and Biochemistry > Collection of Czechoslovak Chemical Communications
Journal or Publication Title:Collection of Czechoslovak Chemical Communications
Volume:56
Number:3
Page Range:pp. 712-717
ISSN:0010-0765
E-ISSN:1212-6950
Publisher:Institute of Organic Chemistry and Biochemistry
Related URLs:
URLURL Type
http://dx.doi.org/10.1135/cccc19910712UNSPECIFIED
ID Code:4987
Item Type:Article
Deposited On:22 Feb 2010 11:27
Last Modified:22 Feb 2010 10:28

Citation

Formelová, Jana; Breier, Albert; Gemeiner, Peter; Kurillová, Lubica (1991) Trypsin entrapped within liposomes. Partition of a low-molecular-mass substrate as the main factor in kinetic control of hydrolysis. Collection of Czechoslovak Chemical Communications, 56 (3). pp. 712-717. ISSN 0010-0765

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