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Biochemistry

Volumn 40, Issue 37, 2001, Pages 11219-11226

Mg2+ binding to alkaline phosphatase correlates with slow changes in protein lability

(3) Dirnbach, E a,b Steel, D G a,b Gafni, A b,c

a UNIVERSITY OF MICHIGAN (United States)

b UNIVERSITY OF MICHIGAN HEALTH SYSTEM (United States)

c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DENATURATION KINETICS;

ESCHERICHIA COLI; ORGANIC COMPOUNDS; PH EFFECTS;

ENZYMES;

ALKALINE PHOSPHATASE; MAGNESIUM ION; ZINC ION; APOENZYME; DIVALENT CATION; GUANIDINE; HOLOENZYME; MAGNESIUM; RECOMBINANT PROTEIN; ZINC;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ESCHERICHIA COLI; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; REACTION ANALYSIS; CHEMICAL MODEL; CHEMICAL STRUCTURE; DRUG EFFECT; ENZYME STABILITY; METABOLISM;

ESCHERICHIA COLI;

ALKALINE PHOSPHATASE; APOENZYMES; CATIONS, DIVALENT; ENZYME STABILITY; GUANIDINE; HOLOENZYMES; MAGNESIUM; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; ZINC;

EID: 0035908887 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi011399m Document Type: Article

Times cited : (12)

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