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Lysosomes from normal rat liver were isolated by affinity chromatography using Sepharose-bound Ricinus communis agglutinins I + II. Characterization of the lysosomal fraction by marker enzymes showed--compared with the homogenate--an enrichment in: acid phosphatase and arylsulfatase about 30- to 60-fold, the tartrate-sensitive acid phosphatase about 95-fold, whereas beta-D-glucosidase, beta-D-galactosidase and sphingomyelinase showed a much higher enrichment of 170- to 260-fold. Marker enzymes for other cell organelles were not detectable. The phospholipid pattern and optical control with electron microscopy gave further indications that the isolated fractions were very rich in lysosomes. A comparison of the phospholipid compositions of plasma membranes isolated from normal rat liver and membranes from the isolated fractions of lysosomes, showed that they were quite different; in particular bis(monoacylglycero)phosphate, which we found to be a typical lysosomal phospholipid, was absent in plasma membranes.
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
February 1976,
FEBS letters,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
September 1974,
FEBS letters,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
April 1984,
Journal of biochemistry,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
February 1981,
Biochemical and biophysical research communications,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
June 1987,
Journal of chromatography,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
January 1983,
Acta physiologica latino americana,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
November 1979,
Biochemical and biophysical research communications,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
September 1976,
Biochemical and biophysical research communications,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
May 1973,
FEBS letters,
F J Kamrath, and
G Dodt, and
H Debuch, and
G Uhlenbruck
December 1978,
FEBS letters,
