PubMed · 1992 · 14 citations · 0 references
Life SciencesBiochemistryMolecular BiologyProtein BiochemistryProteomicsStructural BiologyDisulfide Bond FormationNeurotrophic FactorsProtein DegradationProtein StructureProteolytic EnzymesProteolytic ProcessingDigestionDisulfide Bond AnalysisDisulfide Bond ChemistryDisulfide Bond MispairingDisulfide Bond StructurePeptide MappingProtein Disulfide IsomeraseProteolytic Digestion Analysis
The topology of the disulfides in native heparin-binding neurotrophic factor (HBNF) isolated from bovine brain was studied by proteolytic digestion using trypsin, Asp-N endoproteinase and chymotrypsin and peptide mapping. Disulfide-linked peptides were identified by automated Edman degradation. It has been shown that there are disulfide bonds between Cys15-Cys44, Cys23-Cys53, Cys30-Cys57, Cys67-Cys99 and Cys77-Cys109.