The potentiometric stripping analysis of proteins
β Scribed by Michael J. Honeychurch; Michael J. Ridd
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 783 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1040-0397
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β¦ Synopsis
Abstract
Ten proteins were analyzed by potentiometric stripping analysis (PSA) following reductive accumulation on a HMDE and oxidation with dissolved oxygen. During the reductive accumulation period the surface disulfide bonds are reduced to sulfhydryl pairs. The rate of oxidation of the sulfhydryl pairs is determined by the transport of dissolved oxygen to the electrode surface. Comparison of the PSA response to that obtained by constant current chronopotentiometry (CCCP) of the reduced protein in a deoxygenated solution showed that the presence of dissolved oxygen, in the PSA experiments stabilized the proteins from further conformational changes following the reduction of the surface disulfide bonds.
π SIMILAR VOLUMES
Constant-current enhanced potentlometnc stnppmg analysis (CCEPSA) IS slmdar to potentlometnc stnppmg analysis (PSA) except that durmg the stnppmg step m CCEPSA a cathodic current IS Imposed on the electrode system The freshly oxldlzed metal ions m the vuzunty of the electrode surface are partially r
The determination of Tl(1) by potentiometric stripping analysis (PSA) has been studied. Effects of experimental variables such as the plating, deposition and stirring regimes, and the amount of oxidant are described. After optimization of the relevant experimental variables, an amount of 0.35. lop9