title: [Isolation of highly purified ribonuclease from cobra (Naja oxiana) venom].
abstract: Dialysis, gel-chromatography on Sephadex G-75 (superfine) and chromatography on sulphoethylcellulose give high yield (68 per cent) of 162-fold purified ribonuclease from cobra venom. In ion-exchange chromatography, ribonuclease is eluted in two fractions. The fraction with the highest specific activity has a molecular weight of 15900 and is homogeneous in 15 per cent polyacrilamide gel electrophoresis at pH 8.9. Electrophoresis at pH 4.3 reveals a minor fast component of this fraction which also exhibits a ribonuclease activity. Sulphoethylcellulose chromatography fairly separates cobra venom phosphodiesterase and 5'-nucleotidase eluted as a single fraction in gel chromatography.
mesh_terms: D007527:Isoenzymes / Q000302:isolation & purification; D008970:Molecular Weight; D009708:Nucleotidases / Q000302:isolation & purification; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification; D012260:Ribonucleases / Q000302:isolation & purification*; D012910:Snake Venoms / Q000032:analysis*
chemical_list: D007527:Isoenzymes; D012910:Snake Venoms; D012260:Ribonucleases; D009708:Nucleotidases; D010727:Phosphoric Diester Hydrolases