Immunological detection of single amino acid substitutions in alkaline phosphatase

Science
G T Cocks, A C Wilson

Abstract

Antiserums to wild-type alkaline phosphatase from Escherichia coli were prepared and tested for reactivity with phosphatases altered by point mutations. Eight out of the nine mutant enzymes were distinguished from the wild type with quantitative microcomplement fixation. The structural changes are among the smallest yet observed immunologically.

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