Modification of the properties of bovine pancreatic ribonuclease A by covalent attachment of D-gluconyl-glycine residues.

@article{Biondi1980ModificationOT,
  title={Modification of the properties of bovine pancreatic ribonuclease A by covalent attachment of D-gluconyl-glycine residues.},
  author={L. Biondi and F. Filira and V. Giormani and R. Rocchi},
  journal={International journal of peptide and protein research},
  year={1980},
  volume={15 3},
  pages={
          253-60
        }
}
Bovine pancreatic ribonuclease A was reacted with D-gluconyl-glycine azide in aqueous solution at pH 8.9, in absence of phosphates. Five out of 11 amino groups can be reproducibly modified and the penta D-gluconyl-glycinated ribonuclease A had greater than 70% of the enzymic activity of the unmodified enzyme toward cytidine 2', 3'-cyclic phosphate as well as uridine 2', 3'-cyclic phosphate and yeast RNA. The kinetic parameters Km and k2 of the modified enzyme were calculated from double… Expand
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