Abstract
Abstract Native alkaline phosphatase has been compared with its Zn (II) and Co (II) reconstituted forms by using direct inhibition of enzyme activity by antiserum, quantitative precipitation and serologic analysis with an aqueous polymer phase system. All three of the enzyme forms are differentiable by this combination of methods which allows measurements to be taken at ratios of enzyme and antibody which are in antigen or antibody excess as well as at equivalence. Although difficult to detect by physical techniques, the removal of divalent cations distinctly alters the structure of the enzyme as measured by quantitative precipitin analysis. Data from kinetic studies were interpreted as suggesting that at best, only part of the antibodies bound close to, or directly modified, the enzyme's active site. This was used as supported for the theory that this enzyme must undergo a conformational change in order to catalyze the hydrolysis of substrate.
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