The binding of Na+ to apo-enolase permits the binding of substrate

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1476, Issue 2, 2000, Pages 279-286

  Lin, Tong ^a   Kornblatt, Mary Judith ^a  

^a Gina Cody School of Engineering and Computer Science   (Canada)

Author keywords

Apo enzyme; Enolase; Inactivation; Na+

Indexed keywords

EDETIC ACID; EGTAZIC ACID; ENOLASE; PHOSPHOENOLPYRUVATE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; RABBIT;

ANIMALS; ENZYME ACTIVATION; PHOSPHOPYRUVATE HYDRATASE; PROTEIN BINDING; RABBITS; SODIUM; SUBSTRATE SPECIFICITY;

EID: 0033968662     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00233-2     Document Type: Article

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