Journal of Bacteriology · 1982 · 56 citations · 17 references
Life SciencesBiochemistryMicrobiologyEnzyme MechanismEnzymologyProtein BiochemistryEnzyme BiophysicsEnzyme CharacterizationEnzyme KineticsEnzyme PurificationEnzyme-substrate RecognitionMolecular Weight DeterminationPh Dependence Of Enzyme ActivityPh Effects On Enzyme ActivityPh Effects On EnzymesPhosphatase Enzyme ActivityPhosphatases
Alkaline phosphatase has been purified to homogeneity from two strains of Vibrio cholerae. The enzymes from both strains are single polypeptides of molecular weight 60,000. Both of the enzymes have pH optima around 8.0 and can act on a variety of organic phosphate esters, glucose-1-phosphate being the best substrate. The enzymes are unable to hydrolyze ATP and AMP. Although they have identical Km values, the two enzymes differ significantly in Vmax with p-nitrophenyl phosphate as substrate. The enzymes from the two strains also differ in their sensitivity to EDTA, Pi, and metal ions and activities of the apoenzymes. Ca2+ reactivated the apoenzymes most.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
The Determination of Enzyme Dissociation Constants
Hans Lineweaver, Dean Burk · Journal of the American Chemical Society · 1934 · 12.1K citations