-transparent.png){kind=logo}
The chloroplast 2-oxoglutarate/malate translocator was solubilized from envelope membranes by the detergent n-dodecyl beta-D-maltoside and purified to apparent homogeneity by anion-exchange chromatography followed by gel permeation chromatography. During the purification procedure, the activity of the translocator was monitored by functional reconstitution into phospholipid vesicles. The purified translocator protein has an apparent molecular mass of about 45,000 as revealed by SDS-PAGE. Based on the specific reconstituted transport activity, the purification was about 31-fold with an overall yield of identical to 50%. The substrate specificity of the purified translocator closely resembles that described for the native transport system in intact chloroplasts.
E Menzlaff, and
U I Flügge
August 1998,
Journal of bacteriology,
E Menzlaff, and
U I Flügge
April 1979,
The Journal of biological chemistry,
E Menzlaff, and
U I Flügge
January 2010,
The Plant journal : for cell and molecular biology,
E Menzlaff, and
U I Flügge
June 1974,
FEBS letters,
E Menzlaff, and
U I Flügge
September 1995,
Plant physiology,
E Menzlaff, and
U I Flügge
September 1989,
The Biochemical journal,
E Menzlaff, and
U I Flügge
July 2000,
Plant & cell physiology,
E Menzlaff, and
U I Flügge
February 1974,
Biochimica et biophysica acta,
E Menzlaff, and
U I Flügge
February 1991,
Planta,
E Menzlaff, and
U I Flügge
February 1986,
FEBS letters,
