Folding and activity of mutant cystathionine β-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant

Protein Expression and Purification

Volumn 82, Issue 2, 2012, Pages 317-324

  Majtan, Tomas ^a,b   Kraus, Jan P ^a  

^a UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

^b INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

Affinity chromatography; Cystathionine synthase; Heme; Missense mutation; Protein expression; Protein folding

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; HYBRID PROTEIN; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; ENZYME STABILITY; GENETICS; HEAT; HUMAN; ISOLATION AND PURIFICATION; MOLECULAR CLONING; MOLECULAR GENETICS; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; TRANSITION TEMPERATURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CLONING, MOLECULAR; CYSTATHIONINE BETA-SYNTHASE; ENZYME STABILITY; HOT TEMPERATURE; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; TRANSITION TEMPERATURE;

EID: 84857408197     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2012.01.019     Document Type: Article

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