A METHOD TO STUDY PROTEIN DENATURATION BY MEASUREMENTS OF APPARENT MOLAR VOLUMES
THERMOCHIMICA ACTA, cilt.232, sa.2, ss.297-302, 1994 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 232 Sayı: 2
- Basım Tarihi: 1994
- Doi Numarası: 10.1016/0040-6031(94)80070-7
- Dergi Adı: THERMOCHIMICA ACTA
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.297-302
- Akdeniz Üniversitesi Adresli: Evet
Özet
Protein denaturation was studied by measurements of apparent molar volumes of bovine serum albumin (BSA)-water-urea systems at 25-degrees-C. The viscosity measurements carried out on aqueous BSA solutions at various fixed concentrations as a function of temperature have shown that the denaturation process can best be followed at 60 g kg-1 BSA solution. The apparent molar volumes of urea in water and in 60 g kg-1 BSA solution were measured at 25-degrees-C and the differences between the two were interpreted in terms of structural changes taking place during denaturation of BSA by urea. A simple method was proposed to calculate the volume change per mole of protein upon denaturation. The sample calculation for BSA has shown that there is a volume contraction of 1854 cm3 per mol BSA when the urea concentration reaches 13 M.