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Analysis of the derivative chronopotentiometric peak shape for the reduction of adsorbed bovine serum albumin
Author(s) -
Honeychurch Michael J.,
Ridd Michael J.
Publication year - 1997
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.1140090315
Subject(s) - bovine serum albumin , disulfide bond , adsorption , chemistry , derivative (finance) , inorganic chemistry , chromatography , biochemistry , financial economics , economics
The broad shape of the reduction peak of adsorbed proteins containing multiple electroactive disulfide bonds can be modeled by developing the existing theory used to describe the reduction peaks of proteins with multiple heme groups. This theory is developed and applied to the study of the derivative chronopotentiometric (DCP) reduction peak of adsorbed bovine serum albumin (BSA). For BSA adsorbed on mercury, six disulfide groups were found to be electroactive. It was found that the DCP peak shape could be deconvoluted into five electrochemically equivalent, non‐interacting disulfide groups with formal potentials (vs SCE) of −598 mV, −598 ± 17.8 mV and −598 ± 41.3 mV, and one electrochemically distinct group with a formal potential of −706 mV.