title: Unfolding features of bovine testicular hyaluronidase studied by fluorescence spectroscopy and fourier transformed infrared spectroscopy.
abstract: Chemical unfolding of bovine testicular hyaluronidase (HAase) has been studied by fluorescence spectroscopy and Fourier transformed infrared spectroscopy (FTIR). Thermodynamic parameters were determined for unfolding HAase from changes in the intrinsic fluorescence emission intensity and the formations of several possible unfolding intermediates have been identified. This was further confirmed by representation of fluorescence data in terms of 'phase diagram'. The secondary structures of HAase have been assigned and semiquantitatively estimated from the FTIR. The occurrence of conformational change during chemical unfolding as judged by fluorescence and FTIR spectroscopy indicated that the unfolding of HAase may not follow the typical two-state model.
authors.affiliation: State Key Laboratory of Virology, Department of Biotechnology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
authors.forename: Nina
authors.initials: N
authors.lastname: Pan
authors.forename: Xiaoqiang
authors.initials: X
authors.lastname: Cai
authors.forename: Kai
authors.initials: K
authors.lastname: Tang
authors.forename: Guolin
authors.initials: G
authors.lastname: Zou
mesh_terms: D000818:Animals; D002417:Cattle; D006821:Hyaluronoglucosaminidase / Q000737:chemistry*; D008297:Male; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013737:Testis / Q000201:enzymology*; D013816:Thermodynamics
chemical_list: D006821:Hyaluronoglucosaminidase