RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21569768http://www.w3.org/2000/01/rdf-schema#comment"

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."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.org/dc/terms/identifier"doi:10.1016/j.clinbiochem.2011.04.018"xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Czartoryska B."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Chudy M."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Ziolkowska K."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Brzozka Z."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Dybko A."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/author"Kwapiszewski R."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/name"Clin Biochem"xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/pages"941-943"xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/title"Substrate inhibition of lysosomal hydrolases: alpha-Galactosidase A and beta-glucocerebrosidase."xsd:string
http://purl.uniprot.org/citations/21569768http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/21569768http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21569768
http://purl.uniprot.org/citations/21569768http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21569768
http://purl.uniprot.org/uniprot/#_A0A0S3Q2A7-mappedCitation-21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/#_B4DLT5-mappedCitation-21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/#_P06280-mappedCitation-21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/#_Q53HF3-mappedCitation-21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/#_Q53Y83-mappedCitation-21569768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/Q53HF3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/B4DLT5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/A0A0S3Q2A7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21569768
http://purl.uniprot.org/uniprot/P06280http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21569768