-transparent.png){kind=logo}
Highly purified myelin from rat brain stem has been shown to contain phosphatidate phosphohydrolase, an enzyme which converts phosphatidate to diacylglycerol. The high levels relative to cytosol and microsomes (17% and 22%, respectively) tended to preclude contamination by these fractions as the source of activity. Additional evidence came from study of repeated purification, mixing experiments, and washing of the myelin with salt and detergent. We conclude that this enzyme, in addition to being widely distributed in other subcellular fractions, is intrinsic to the myelin membrane. Through its activity it generates a key substrate for the cytidine (Kennedy) pathway which was previously shown to occur in this membrane.
K K Vaswani, and
R W Ledeen
December 1983,
Neurochemical research,
K K Vaswani, and
R W Ledeen
March 1996,
FEBS letters,
K K Vaswani, and
R W Ledeen
August 1994,
The Biochemical journal,
K K Vaswani, and
R W Ledeen
October 1989,
The Biochemical journal,
K K Vaswani, and
R W Ledeen
July 1965,
Biochimica et biophysica acta,
K K Vaswani, and
R W Ledeen
January 1971,
European journal of biochemistry,
K K Vaswani, and
R W Ledeen
May 1996,
Chemistry and physics of lipids,
K K Vaswani, and
R W Ledeen
June 1992,
Biochimica et biophysica acta,
K K Vaswani, and
R W Ledeen
March 1969,
Comparative biochemistry and physiology,
K K Vaswani, and
R W Ledeen
March 1980,
Biochemical pharmacology,
