Ribonuclease from cobra snake venom: purification by affinity chromatography and further characterization.
A ribonuclease from cobra snake venom was isolated and purified to homogeneity using antibody-affinity chromatography, increasing the yield fourfold. The purified enzyme showed cytidylic acid specificity, as reported earlier. Further, the effects of temperature, pH, metal ions, inhibitors, and urea on the enzyme activity were studied. Snake venom RNase exhibited salt-dependent reversible association-dissociation behaviour. Immunological studies indicate that this enzyme shares one of the antigenic sites of RNase A. The partial N-terminal sequence of the enzyme showed considerable homology with phospholipases from snake venom; however, the enzyme itself did not show any phospholipase activity.
Mahalakshmi
Y V
YV
Centre for Cellular and Molecular Biology, Hyderabad, India.
Jagannadham
M V
MV
Pandit
M W
MW
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D018899:CpG Islands; D003568:Cytidine Monophosphate / Q000378:metabolism; D004546:Elapid Venoms / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007477:Ions; D008969:Molecular Sequence Data; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification*; D012492:Salts / Q000378:metabolism; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014508:Urea / Q000494:pharmacology
D004546:Elapid Venoms; D007477:Ions; D012492:Salts; D014508:Urea; D012260:Ribonucleases; D003568:Cytidine Monophosphate