Calcium, magnesium and the conformation of parvalbumin during muscular activity.

Abstract:

:The conformation of perch parvalbumin in the Ca-, Mg- and metal-free state was studied by intrinsic fluorescence, trypsin susceptibility, thiol titration and circular dichroism. The data reveal that Ca-parvalbumin has a more compact structure than the metal-free protein, with a high alpha-helical content and a buried thiol. No difference in conformation could be detected between Mg- and Ca-parvalvumin, indicating that the Ca-Mg exchange that may take place during muscular activity is accompanied by little or no structural changes. Furthermore, recently published kinetic parameters can now be interpreted as meaning that, during the contraction-relaxation cycle, parvalbumin often stays in the Mg-form instead of switching to the Ca-form which is predominant in vitro.

journal_name

Biochimie

journal_title

Biochimie

authors

Cox JA,Winge DR,Stein EA

doi

10.1016/s0300-9084(79)80157-1

subject

Has Abstract

pub_date

1979-01-01 00:00:00

pages

601-5

issue

5-6

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(79)80157-1

journal_volume

61

pub_type

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