Abstract
Analysis of amino acid composition of extracellular RNAase from B. subtilis demonstrated that it differed strikingly from bovine pancreatic RNAase in that it contained trytophan instead of cysteine. Fingerprinting of peptides obtained by proteolytic digestion showed that the spots given by B. subtilis RNAase were all different from those given by bovine pancreatic RNAase. Photooxidation of B. subtilis RNAase in the presence of methylene blue resulted in a complete inactivation of this RNAase accompanied by a specific decrease of histidine residue in the molecule, a result which suggested that histidine played an important role in the catalytic activity of this RNAase. RNAase activity was completely lost by titration with N-bromosuccinimide, but alkylating agents, such as iodoacetic or bromoacetic acid, did not react with the RNAase under any of the conditions tested.
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