Verification of protein disulfide bond arrangement by ingel tryptic digestion under entirely neutral pH conditions

摘要

To develop a concise proteomic procedure to verify the protein disulfide bond arrangement, non-reductive trypsin digestion of neuregulin 1-?l (176-246), a model disulfide-containing protein, was assessed by a proteolytic 180-labeling analysis. As a result, the commonly used in-gel tryptic digestion method has been improved for use entirely under neutral pH conditions. With this procedure, the disulfide arrangement of proteins could represent a clinical index candidate in pathological proteomic studies.