Pyrococcus abyssi alkaline phosphatase: The dimer is the active form

Journal of Inorganic Biochemistry

Volumn 98, Issue 4, 2004, Pages 575-581

  Zappa, S ^a   Boudrant, J ^a   Kantrowitz, E R ^b  

^a CNRS   (France)

^b BOSTON COLLEGE   (United States)

Author keywords

Alkaline phosphatase; Metalloenzyme; Pyrococcus abyssi; Thermostable enzyme

Indexed keywords

ALKALINE PHOSPHATASE; BUFFER; DIMER; METAL; MONOMER; POTASSIUM DIHYDROGEN PHOSPHATE; TROMETAMOL;

ACIDITY; ARTICLE; CHEMICAL COMPOSITION; CONTROLLED STUDY; DISSOCIATION; ENZYME BINDING; ENZYME ISOLATION; ENZYME STABILITY; ENZYME STRUCTURE; EXPERIMENT; METAL BINDING; NONHUMAN; PARAMETER; PH; PROTEIN ASSEMBLY; PYROCOCCUS ABYSSI; STRUCTURE ANALYSIS;

ALKALINE PHOSPHATASE; CENTRIFUGATION, DENSITY GRADIENT; CIRCULAR DICHROISM; DIMERIZATION; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; METALS; PROTEIN STRUCTURE, QUATERNARY; PYROCOCCUS; STRUCTURE-ACTIVITY RELATIONSHIP;

PYROCOCCUS; PYROCOCCUS ABYSSI;

EID: 1642386872     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2004.01.009     Document Type: Article

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