[Synthesis and properties of an affinity adsorbent for purifying neuraminidases of varying origins].

Neuraminidases (NA) from Clostridium perfringens, noncholera vibrios and influenza virus were purified by affinity chromatography on Sepharose coupled to para-aminophenyl oxamic acid. Adsorption was carried out at pH 5.5. The effect of elution conditions on purification of NA was studied. The use of the pH gradient enhances 10-fold the purification degree as compared with the pH shift-elution process, 90% of the activity being eluted from the column within a pH range from 6.0 to 6.6. According to the described procedure, electrophoretically homogeneous preparations of NA were obtained from noncholera vibrios and influenza virus.