Abstract
Summary A selective adsorbent for neuraminidase was prepared by attaching through azo linkage an inhibitor of this enzyme, N-(p-aminophenyl) oxamic acid, to agarose beads containing the tripeptide, glycyl-glycyl-tyrosine. Columns containing this adsorbent can completely extract the enzymatic activity present in extracts of Clostridium perfringens and Vibrio cholerae , and quantitative elution is readily achieved by modifying the pH and ionic strength of the buffer. Intact influenza virus particles are also reversibly adsorbed by these columns, indicating the superficial location of neuraminidase in this virus and emphasizing the feasibility of using functional purification procedures for resolving complex and particulate biological structures.
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