sodium-dodecyl-sulfate and alpha-sarcin

The substrate specificity of monomeric and dimeric forms of alpha-sarcin was investigated by membrane blotting procedures. Dimeric alpha-sarcin fails to inactivate ribosomes as well as to hydrolyze mini-stem-loop RNA, whereas monomeric alpha-sarcin catalyzes both substrates. Both monomeric and dimeric alpha-sarcin are effective ribonucleases that are displayed by in situ RNA-impregnated gel electrophoresis. The same purine base specificity was detected for both dimeric and monomeric forms. alpha-Sarcin is also an effective deoxyribonuclease to supercoiled DNA. The action of alpha-sarcin as deoxyribonuclease and ribonuclease is inhibited by the presence of SDS (3.5 x 10(-6) M); the inhibition on ribonuclease, but not on deoxyribonuclease, is reversible if the proteins are renatured.

Topics: Animals; Base Composition; DNA; Endoribonucleases; Fungal Proteins; Membranes, Artificial; Polyvinyls; Protein Binding; Protein Conformation; Rabbits; Rats; Ribosomes; RNA; RNA, Ribosomal, 5S; Sodium Dodecyl Sulfate; Substrate Specificity