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The primary structure of muskrat pancreatic rnase


, : The primary structure of muskrat pancreatic rnase. International Journal of Peptide and Protein Research 8(3): 305-316

Pancreatic RNase from Ondatra zibethica was isolated and its amino acid sequence was determined from tryptic digests of the performic acid-oxidized and the reduced and aminoethylated enzyme. The peptides were positioned in the sequence by homology with other RNases. This could be done unambiguously for all peptides except Arg-Arg (tentative position 32-33) and ser-Arg (tentative position 75-76). The amino acid sequences of the peptides were determined by the dansyl-Edman method, with the exception of residues 23-25 and 99-102, which were positioned by homology. The enzyme differs in 38 positions from the enzyme from rat and in 31-42 positions from other mammalian pancreatic RNases, while rat ribonuclease differs at 44-52 positions from the other enzymes. These data point to a common ancestry of the enzymes from muskrat and rat and an increased evolution rate of rat RNase after divergence of the ancestors of both species. Muskrat RNase contains no carbohydrate, although the enzyme possesses a recognition site for carbohydrate attachment in the sequence Asn-Val-Thr (62-64).

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