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
Biochimiejournal_title
Biochimieauthors
Cox JA,Winge DR,Stein EAdoi
10.1016/s0300-9084(79)80157-1subject
Has Abstractpub_date
1979-01-01 00:00:00pages
601-5issue
5-6eissn
0300-9084issn
1638-6183pii
S0300-9084(79)80157-1journal_volume
61pub_type
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