Literature DB >> 21569768

Substrate inhibition of lysosomal hydrolases: α-Galactosidase A and β-glucocerebrosidase.

Radoslaw Kwapiszewski1, Barbara Czartoryska, Karina Ziolkowska, Michal Chudy, Artur Dybko, Zbigniew Brzozka.   

Abstract

OBJECTIVE: We have investigated the kinetics of α-galactosidase A and β-glucocerebrosidase deficient in Fabry and Gaucher diseases, respectively. DESIGN AND METHODS: We have performed spectrofluorymetric measurements of the activity of enzymes using a derivative of 4-methylumbelliferone as a substrate and a human T-cell line as a source of enzymes.
RESULTS: We have observed the substrate inhibition effect, which is related to temperature.
CONCLUSIONS: The diagnostic procedures for Fabry and Gaucher diseases used now in laboratory practice neglect temperature-dependent substrate inhibition, which may significantly reduce the sensitivity of enzyme activity determinations.
Copyright © 2011 The Canadian Society of Clinical Chemists. Published by Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21569768     DOI: 10.1016/j.clinbiochem.2011.04.018

Source DB:  PubMed          Journal:  Clin Biochem        ISSN: 0009-9120            Impact factor:   3.281


  2 in total

1.  Determination of Acid β-Galactosidase Activity: Methodology and Perspectives.

Authors:  Radoslaw Kwapiszewski; Justyna Szczudlowska; Karina Kwapiszewska; Michal Chudy; Zbigniew Brzozka
Journal:  Indian J Clin Biochem       Date:  2013-03-28

2.  Effect of a high surface-to-volume ratio on fluorescence-based assays.

Authors:  Radoslaw Kwapiszewski; Karina Ziolkowska; Kamil Zukowski; Michal Chudy; Artur Dybko; Zbigniew Brzozka
Journal:  Anal Bioanal Chem       Date:  2012-02-12       Impact factor: 4.142

  2 in total

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