4.50—Polarographic investigation of conformational changes of human serum albumin: Part I. Unfolding of human serum albumin by urea |
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Authors: | Josef Chmelik Vitěz Kalous |
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Affiliation: | Department of Physical Chemistry, Charles University, Albertov 2030, 128 40 Prague 2 Czechoslovakia |
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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 Brdi?ka 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. |
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