INTERACTION BETWEEN AROMATIC ESTERASE OF HUMAN SERUM AND BIVALENT METAL IONS

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Abstract
Calcium, magnesium, and manganese ions were tested for influences on aromatic esterase activity of Harvard fraction IV-1 of human serum. The metals altered the Michaelis constant of the enzyme substrate complex as well as the maximum rate of hydrolysis. The metal ions and the active centers in the enzyme seemed to combine in a ratio of 1:1, and similarly one molecule of substrate was bound to one active center. Activating and inhibiting metals seemed to compete with each other for the same center of the esterase.