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Journal / Biochemistry / Espressione, purificazione, cristallizzazione e…
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Biochemistry

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JoVE Journal Biochemistry
Espressione, purificazione, cristallizzazione e saggi enzimatici di Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Journal (Biochemistry)
Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Journal (Biochemistry)
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
 
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Espressione, purificazione, cristallizzazione e saggi enzimatici di Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Article DOI: 10.3791/59729-v • 10:21 min • June 20th, 2019
June 20th, 2019 •
1,2, 1,2, 1,2, 1, 1, 3, 3, 4, 1,2
1Research Institute for Biomedical Aging Research, University of Innsbruck Austria, 2Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck Austria, 3Division of Genetic Epidemiology, Medical University of Innsbruck Austria, 4Faculty of Chemistry, Department of Organic Chemistry, University of Vienna Austria

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L'espressione e la purificazione delle proteine contenenti idrolasi fumarylacetoacetate sono descritte con esempi (espressione in E. coli, FPLC). Le proteine purificate sono utilizzate per la cristallizzazione e la produzione di anticorpi e impiegate per i saggi enzimatici. Vengono presentati alcuni saggi fotometrici per mostrare la multifunzionalità di FAHD1 come oxaloacetate decarboxylase e idrolasi acylpyruvate.

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Biochimica Numero 148 FAH FAHD FAHD1 ODx ApH idrolame decarboxylase oxaloacetate acetilpyruvate acylpyruvate ossalato piratosa MiDAS
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