Abstract
At enzyme concentrations above 40 nM the configuration of the purified plasma membrane Ca2+-ATPase is that of calmodulin-insensitive dimers. Dilution of the enzyme generates progressively higher proportions of calmodulin-sensitive monomers with lower Vmax and Ca2+ sensitivity than the dimeric enzyme. Dimerization from monomeric state had not been documented before. We investigated whether concentration by volume exclusion, obtained by addition of a large molecular weight dextran to a monomeric Ca2+-ATPase would elicit dimer-like behavior. Dextran induced self-association of monomers, as monitored by fluorescence energy transfer, but the Ca2+ sensitivity of the re-associated monomers was lower than that of the native dimers. These results suggest that the self-association reaction is structurally but not functionally reversible, and also document the existence of a hitherto unknown kinetic state of the oligomerized Ca2+-ATPase, with high Vmax but low Ca2+-sensitivity.
Original language | English (US) |
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Pages (from-to) | 57-60 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 371 |
Issue number | 1 |
DOIs | |
State | Published - Aug 28 1995 |
Externally published | Yes |
Keywords
- Ca-ATPase
- Dextran
- Enzyme activation
- Oligomerization
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology