Abstract
Adenylate cyclase from bovine brain cortex was reconstituted into liposomes with (1000 fold) or without transmembrane Ca2+ gradient. The highest enzyme activity (the active center of enzyme exposing outside) was observed in the vesicles with lower Ca2+ concentration outside (≈10-6 M, similar to physiological condition). If the transmembrane Ca2+ gradient was in the inverse direction (i.e. higher Ca2+ concentration outside, 1 mM), a lowest enzyme activity would appear. Such a difference could be diminished following addition of A23187. Obtained results showed that a proper transmembrane Ca2+ gradient is essential for the optimal fluidity of phospholipid bilayer, favouring the formation of suitable conformation of adenylate cyclase with higher enzyme activity.
Original language | English (US) |
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Pages (from-to) | 366-371 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 175 |
Issue number | 2 |
DOIs | |
State | Published - Mar 15 1991 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology