Abstract
The identification of a protein drug and the determination of its purity requires the use of several analytical methods. One identification probe used is the proteolysis of insulin with Staphylococcus aureus protease. This method yields a characteristic pattern of peptide fragments (“fingerprint”) which could be separated by reverse-phase high-performance liquid chromatography (HPLC) with gradient elution and ultraviolet detection. This probe could be used as a stability-indicating method for peptide and proteins, supplementing other traditional methods as reverse-phase (RP) and size-exclusion (SE) HPLC. Proteolysis of commercial human insulin preparations stored under different conditions produces modified fingerprints versus reference standard digested samples. Results vary as a function of the type of preparation and storage conditions since the degradation products detected by SE-HPLC are different.
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