On the Structure of Bovine Pancreatic Ribonuclease B. Isolation of a Glycopeptide
Ribonuclease B is a constituent of the zymogen granules of bovine pancreatic acinar cells and is secreted in the pancreatic juice of cattle. Its isolation from bovine pancreatic juice has been described. The enzyme is a glycoprotein that possesses an amino acid composition indistinguishable from that of ribonuclease A and contains carbohydrate to the extent of six residues of mannose and two residues of glucosamine per molecule. The experiments to be described in the present communication were designed to provide preliminary structural information about the protein, and, in particular, to furnish an understanding of the distribution of the carbohydrate in the molecule. The experiments have demonstrated that the carbohydrate content is accounted for by a single covalently-bonded oligosaccharide moiety attached at an aspartic acid or asparagine residue, and have provided further presumptive evidence that the structure of the protein is otherwise identical to that of ribonuclease A. (auth)
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- US Atomic Energy Commission (AEC)
- DOE Contract Number:
- AT(30-2)-GEN-16
- OSTI ID:
- 12491957
- Report Number(s):
- BNL-7788
- Journal Information:
- Journal of Biological Chemistry, Vol. 239; ISSN 0021-9258
- Publisher:
- American Society for Biochemistry and Molecular Biology
- Country of Publication:
- United States
- Language:
- English
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