Inactivation and conformational changes of yeast invertase during unfolding in urea and guanidinium chloride solutions.
Yeast invertase exists in two different forms. The cytoplasmic enzyme is non-glycosylated, whereas the external invertase contains approximately 50% carbohydrate of the high mannose type. In this paper, the inactivation and the conformational changes of the yeast external invertase are analyzed for unfolding in urea and guanidinium chloride. The results show that much lower concentrations of denaturants are required to bring about inactivation than are required to produce significant conformational changes of the yeast external invertase. The results suggest that the active sites of the external invertase containing carbohydrate residues may display more conformational flexibility than the enzyme molecules as a whole.
Li
S
S
Department of Biological Science and Biotechnology, Tsinghua University, Beijing, China.
Yang
H P
HP
Zhou
H M
HM
D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D019791:Guanidine / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D014508:Urea / Q000737:chemistry*; D043324:beta-Fructofuranosidase
D014508:Urea; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D019791:Guanidine