Selective Isolation ofVibrio choleraeNeuraminidase using an Immobilized 4-(Nitrophenyl)oxamic Acid

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Abstract
N-(4-Nitrophenyl)oxamic acid was coupled with Sepharose 4B containing 1,6-diaminohexane as spacer group. This material was used as a specific adsorbent in the purification of V. cholerae neuraminidase [EC 3.2.1.18]. The enzyme was completely retarded and separated from the bulk of the protein when washed with 50 mM sodium acetate buffer, pH 5.0. A stepwise increase of NaCl concentration from 1.0 to 2.0 M was necessary for a sharp elution of neuraminidase activity. The purification was 10-fold, and a recovery of > 90% was obtained. Neuraminidase is weakly retarded on a column of 1,6-diaminohexane coupled with Sepharose 4B and is not adsorbed by Sepharose 4B.