Abstract
Porcine mitochondrial malate dehydrogenase (EC 1.1.1.37) dissociates into subunits on dilution. The enzyme monomer caused large increases in the surface pressure of monolayers of 1:1 phosphatidylserine/phosphatidylcholine at air/water and oil/water interfaces. The monomer increased the permeability of phospholipid vesicles to 22Na+. Both effects were significantly greater than the corresponding effects of ribonuclease A, cytochrome c and the dimeric form of malate dehydrogenase. Changes in the circular-dichroism spectra of the enzyme indicated that conformational changes may be associated with dimer formation or when monomer interacts with lysophosphatidyl-choline. Similar interactions to those described may occur in situ when mitochondrial malate dehydrogenase is transported to the mitochondrial matrix from its site of synthesis on cytosolic ribosomes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 227-233 |
| Number of pages | 7 |
| Journal | The Biochemical journal |
| Volume | 186 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 15 1980 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology