Bison pancreatic ribonuclease was isolated by affinity chromatography. Thermolysin and tryptic digestion of denaturated protein, and subtilisin digestion of native protein yielded peptides, which were purified and submitted to amino acid analysis. These peptides, together with partial sequence data obtained by Stewart & Stevenson (16) overlap the entire amino acid sequence of bison ribonuclease. No differences with bovine ribonuclease were found, although there may be differences in state of amidation of some residues.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Bison pancreatic ribonuclease was isolated by affinity chromatography. Thermolysin and tryptic digestion of denaturated protein, and subtilisin digestion of native protein yielded peptides, which were purified and submitted to amino acid analysis. These peptides, together with partial sequence data obtained by Stewart & Stevenson (16) overlap the entire amino acid sequence of bison ribonuclease. No differences with bovine ribonuclease were found, although there may be differences in state of amidation of some residues.
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| skos:exactMatch | |
| uniprot:name |
Int. J. Pept. Protein Res.
|
| uniprot:author |
Beintema J.J.,
Muskiet F.A.J.,
Welling G.W.
|
| uniprot:date |
1976
|
| uniprot:pages |
345-348
|
| uniprot:title |
Studies on the primary structure of bison pancreatic ribonuclease.
|
| uniprot:volume |
8
|