[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.
Poltorak
A N
AN
Martiushin
S V
SV
Pasechnik
V A
VA
D000327:Adsorption; D000345:Affinity Labels / Q000138:chemical synthesis*; D002846:Chromatography, Affinity / Q000379:methods; D003016:Clostridium perfringens / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D009980:Influenza A virus / Q000201:enzymology; D008024:Ligands; D009439:Neuraminidase / Q000302:isolation & purification*; D010072:Oxamic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D014733:Vibrio / Q000201:enzymology; D014734:Vibrio cholerae / Q000201:enzymology
D000345:Affinity Labels; D008024:Ligands; C046766:4-aminophenyloxamic acid; D009439:Neuraminidase; D010072:Oxamic Acid
Sintez i svoĭstva affinnogo adsorbenta dlia ochistki neĭraminidaz razlichnogo proiskhozhdeniia.