title: Protein denaturation in dosage forms measured by differential scanning calorimetry.
abstract: The stability of beta-galactosidase dosage forms was studied by differential scanning calorimetry (DSC). It was found that the observed enthalpy of thermal denaturation was approximately in proportion to remaining enzyme activity, and denaturation temperature was related to protein stability. These results suggest that DSC can be used to determine native proteins in dosage forms and to clarify the factors affecting protein stability. The DSC method seems to be more convenient than conventional activity assay methods, and useful to follow protein denaturation during the manufacturing process and storage of dosage forms.
authors.affiliation: National Institute of Hygienic Science, Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Izutsu
authors.forename: S
authors.initials: S
authors.lastname: Yoshioka
authors.forename: Y
authors.initials: Y
authors.lastname: Takeda
mesh_terms: D002152:Calorimetry, Differential Scanning; D004355:Drug Stability; D005696:Galactosidases / Q000032:analysis*; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis*
chemical_list: D011506:Proteins; D005696:Galactosidases