Stabilities of uncomplemented and complemented M15 β-galactosidase (Escherichia coli) and the relationship to α-complementation

Biochemistry and Cell Biology

Volumn 77, Issue 2, 1999, Pages 109-118

  Gallagher, Clare N ^a   Huber, Reuben E ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

complementation; galactosidase; Stability

Indexed keywords

BETA GALACTOSIDASE; DIMER; MAGNESIUM ION; MERCAPTOETHANOL; MUTANT PROTEIN; OLIGOMER; SODIUM ION; UREA;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIMERIZATION; ENZYME BINDING; ENZYME DENATURATION; ENZYME STABILITY; NONHUMAN; PRECIPITATION; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; REACTION ANALYSIS; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ALPHA-GALACTOSIDASE; BETA-GALACTOSIDASE; ENZYME STABILITY; ESCHERICHIA COLI; HEATING; MAGNESIUM; MERCAPTOETHANOL; PROTEIN CONFORMATION; SODIUM CHLORIDE; TEMPERATURE;

ESCHERICHIA COLI;

EID: 0032842665     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/bcb-77-2-109     Document Type: Article

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