PT  - JOURNAL ARTICLE
AU  - Reese, R. T.
AU  - Treffers, H. P.
TI  - The Effects of Specific Metals on the Antigenic Structure of Alkaline Phosphatase from Escherichia Coli
DP  - 1973 Jan 01
TA  - The Journal of Immunology
PG  - 10--20
VI  - 110
IP  - 1
4099  - http://www.jimmunol.org/content/110/1/10.short
4100  - http://www.jimmunol.org/content/110/1/10.full
SO  - J. Immunol.1973 Jan 01; 110
AB  - 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.