An Evaluation of the Average Heats of Ionization of Reduced and Oxidized Horse Heart Cytochrome c
作者:
MarioA. Marini,
CharlesJ. Martin,
RobertL. Berger,
期刊:
Analytical Letters
(Taylor Available online 1979)
卷期:
Volume 12,
issue 11
页码: 1137-1147
ISSN:0003-2719
年代: 1979
DOI:10.1080/00032717908067904
出版商: Taylor & Francis Group
关键词: cytochromec;heats of ionization;redox forms
数据来源: Taylor
摘要:
Evaluation of the average heats of ionization ΔHi.) for oxidized and reduced horse heart cytochrome c reveals that the heats of ionization for both redox species as a function of pH are identical within the precision of the method. Since this result is obtained in spite of the differences in the numbers of groups titrated in the two forms of the protein, the redox forms must have the same heats of ionization per group titrated. When the heats of ionization are plotted as a function of the groups titrated, the differences are more clearly seen. For proteins with one or two imidazoyl ionizations between many carboxyl and ε-amino ionizations, there is no clearly indicated plateau and the heats of ionization of the imidazole groups of histidines cannot be obtained by this procedure. The analysis is, however, useful for eliminating heats of ionization which are abnormal since the shape of the calculated curves are at variance with the experimental data.
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