Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes.

K. A. Webster, K. B. Freeman, S. Ohki

Research output: Contribution to journalArticle

4 Scopus citations

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 languageEnglish (US)
Pages (from-to)227-233
Number of pages7
JournalThe Biochemical journal
Volume186
Issue number1
DOIs
StatePublished - Jan 15 1980

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes.'. Together they form a unique fingerprint.

  • Cite this