Ca2+-binding of S-100 protein in the presence of K+ and Mg2+.

Abstract:

:Ca2+-binding of S-100 protein was studied using a Ca2+ electrode at pH 6.80. In the presence of 0.1 M KCl and 10 mM MgCl2 (ionic strength 0.13), Ca2+-binding to S-100 protein occurred in three steps with positive cooperativity. The numbers of bound Ca2+ ions in the three steps were 2, 2, and 4. The Ca2+-binding constants were 6.9 x 10(3) M-1, 2.9 x 10(3) M-1, and 3.7 x 10(2) M-1, respectively. The Ca2+-binding constants of the first and second steps obtained in the presence of 33.3 mM MgCl2 or 0.1 M KCl (ionic strength 0.10) were 1.4 times larger than those described above. This suggests that Mg2+ does not inhibit Ca2+-binding of S-100 protein. The increase of KCl concentration from 0.1 to 0.2 M caused a decrease of the Ca2+-binding constants to ca. 50%.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Matsuda S

doi

10.1093/oxfordjournals.jbchem.a122596

subject

Has Abstract

pub_date

1988-12-01 00:00:00

pages

989-90

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

104

pub_type

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