Venom exonuclease. III. Immunochemical characterization and modification by specific antibody.
The immunoelectrophoretic purity of the exonuclease preparation, isolated from Crotalus adamanteus venom according to a procedure previously published (Dolapchiev, L.B., Sulkowski, E. and Laskowski, M., Sr. (1974) Biochem. Biophys. Res. Commun. 61, 271-281), is reported. The enzyme showed one precipitin line against antibody prepared against partially purified venom. The exonuclease is unstable in dilute (1.25 microgram/ml and below) solutions. Bovine serum albumin stabilized the enzyme nonspecifically whereas the homologous antibody demonstrated a specific stabilizing effect under the same conditions. The binding of the anti-enzyme with the enzyme caused inhibition of both its activities--phosphodiesterase and pyrophosphatase. The inhibition of the exonuclease when attacking high molecular weight substrates is similar to the above and is of the same noncompetitive type. The thermal stability of venom exonuclease is reported.
D000818:Animals; D000917:Antibody Formation; D000937:Antigen-Antibody Reactions; D003435:Crotalid Venoms / Q000276:immunology*; D004355:Drug Stability; D005092:Exonucleases / Q000037:antagonists & inhibitors / Q000276:immunology*; D007106:Immune Sera; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D011817:Rabbits / Q000276:immunology; D005719:gamma-Globulins / Q000302:isolation & purification
D003435:Crotalid Venoms; D007106:Immune Sera; D005719:gamma-Globulins; D005092:Exonucleases