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Thermostability Measurement of an α-Glucosidase Using a Classical Activity-based Assay and a Novel Thermofluor Method.
Ernits, Karin; Viigand, Katrin; Visnapuu, Triinu; Põsnograjeva, Kristina; Alamäe, Tiina.
Afiliação
  • Ernits K; Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
  • Viigand K; Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
  • Visnapuu T; Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
  • Põsnograjeva K; Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
  • Alamäe T; Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Bio Protoc ; 7(12): e2349, 2017 Jun 20.
Article em En | MEDLINE | ID: mdl-34541099
ABSTRACT
α-glucosidases (including maltases and isomaltases) are enzymes which release glucose from a set of α-glucosidic substrates. Their catalytic activity, substrate specificity and thermostability can be assayed using this trait. Thermostability of proteins can also be determined using a high-throughput differential scanning fluorometry method, also named Thermofluor. We have shown that Thermofluor can also be applied to predict binding of substrates and inhibitors to a yeast α-glucosidase. The methods described here in detail were used in Viigand et al., 2016 .
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Texto completo: 1 Bases de dados: MEDLINE Idioma: En Revista: Bio Protoc Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estônia

Texto completo: 1 Bases de dados: MEDLINE Idioma: En Revista: Bio Protoc Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estônia