Abstract
The primary structure of the main component of whale pancreatic ribonuclease (RNase W1) was studied. The N-terminal amino acid was not found by conventional techniques and was assumed to be Nα-blocked lysine. The C-terminal amino acid was identified as valine. The peptides obtained by cleavage with cyanogen bromide, trypsin, and chymotrypsin were separated by Sephadex G-25 or Dowex 50 X-2 column chromatography and purified by means of paper chromatography or paper electrophoresis. The amino acid sequences of some of the peptides were determined by the Edman-dansyl procedure. It was found that RNase W1 includes sequences closely similar to those around the active site of ribonuclease A [EC 2. 7. 7. 16] (His-12, Lys-41, and His-119) and their correlation with the enzymatic activity was discussed.
