Publication | Open Access
Bovine pancreatic deoxyribonuclease A. Isolation of cyanogen bromide peptides; complete covalent structure of the polypeptide chain.
106
Citations
17
References
1992
Year
Half-cystine ResiduesBioorganic ChemistryAldo-keto ReductaseGlycobiologyMolecular BiologyPeptide SciencePolypeptide ChainComplete Covalent StructureChemical BiologyEnzymatic ModificationRedox BiologyBiosynthesisStructure-function Enzyme KineticsBiochemistryBiomolecular EngineeringSecondary SiteCellular EnzymologyNatural SciencesEnzyme CatalysisPeptide TherapeuticPeptide SynthesisProtein EngineeringCarbohydrate MoietyMedicineCyanogen Bromide Peptides
Abstract The following sequence and the pairing of the half-cystine residues has been derived for bovine pancreatic deoxyribonuclease A. [see PDF for sequence] The sequence permits the following assignments of residues known to have special properties. The carbohydrate moiety is attached to Asn18. The crucial histidine residue subject to alkylation by iodoacetate is His131. The site of nitration when the enzyme is inactivated by tetranitromethane is Tyr62; the secondary site of nitration is Tyr73. The essential disulfide bond links residues 170 and 206.
| Year | Citations | |
|---|---|---|
Page 1
Page 1