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 |
|---|---|
| Pages (from-to) | 227-233 |
| Number of pages | 7 |
| Journal | Biochemical Journal |
| Volume | 186 |
| Issue number | 1 |
| State | Published - Jan 15 1980 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes. / Webster, Keith A; Freeman, K. B.; Ohki, S.
In: Biochemical Journal, Vol. 186, No. 1, 15.01.1980, p. 227-233.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes.
AU - Webster, Keith A
AU - Freeman, K. B.
AU - Ohki, S.
PY - 1980/1/15
Y1 - 1980/1/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0019324505&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019324505&partnerID=8YFLogxK
M3 - Article
C2 - 7370011
AN - SCOPUS:0019324505
VL - 186
SP - 227
EP - 233
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 1
ER -