HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Reese, R. T. Articles by Treffers, H. P. Search for Related Content PubMed Articles by Reese, R. T. Articles by Treffers, H. P.

The Effects of Specific Metals on the Antigenic Structure of Alkaline Phosphatase from Escherichia Coli

From the Department of Microbiology, Yale University, New Haven, Connecticut 06510

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.

Footnotes

¹ Present address: Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218.