|
|||||
|
|
Polarographic investigation of conformational changes of human serum albumin: Part I. Unfolding of human serum albumin by urea |
|
| Affiliation: | 2. Department of Mechanical and Materials Engineering, University of Cincinnati, Cincinnati, OH, United States;3. Department of Physics, University of Cincinnati, Cincinnati, OH, United States;4. Department of Chemical and Environmental Engineering, University of Cincinnati, Cincinnati, OH, United States |
| Abstract: | The mechanism of the unfolding of human serum albumin by urea was studied using d. c. polarography. It was found that this reaction is a complex process which cannot be described in terms of a two-state transition model. As well as the Brdička catalytic current we have also studied the reduction current of disulfide groups in native and denatured human serum albumin. The number of cystine residues accessible for electrode reduction in native and denatured protein was calculated. On the basis of these results a scheme for the unfolding of human serum albumin by urea is proposed. |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ | |