Tissue fractionation studies. 18. Resolution of mitochondrial fractions from rat liver into three distinct populations of cytoplasmic particles by means of density equilibration in various gradients

Beaufay, Henri; Jacques, P. J.; Baudhuin, Pierre; Sellinger, O. Z.; Berthet, J; Duve, Christian de

doi:10.1042/bj0920184

Cited by 337 publications

(155 citation statements)

References 15 publications

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“…However, the highest specific activity of the enzyme was always found in those fractions which were enriched with lysosomes. In addition, the guinea-pig enzyme followed a shift in lysosomal density when the animals were injected with the non-ionic detergent Triton WR-1339, a finding considered conclusive evidence of a lysosomal location (see Beaufay, 1972). However, the location of the rat enzyme is less obvious from our results.…”

Section: Discussionsupporting

confidence: 45%

“…have also noted that some particles containing acid hydrolases sedimented from mucosal homogenates at low centrifugal forces. Perhaps the situation in the intestine is somewhat analogous to that in the liver where acid phosphatase and acid DNAase are contained in different populations of lysosomes (Beaufay et al, 1964).…”

Section: Discussionmentioning

confidence: 98%

“…Since lysosomes have been repeatedly seen in the epithelial cells ofrat intestine (Behnke & Moe, 1964;Moe et al, 1965;Trier, 1968), it is puzzling that acid hydrolases from these cells did not display the behaviour expected for lysosomal enzymes. Possibly this indicates that the granules in this tissue were more easily damaged by the manipulations used to prepare the tissue fractions than those from guinea-pig epithelium, since it is recognized that lysosomes from different sources vary greatly in their fragility (Turnbull & Neil, 1969;Beaufay, 1972;Reid, 1972). Hsu & Tappel (1964) have reported that intestinal epithelium, in common with kidney (Straus, 1956), contains a more heterogeneous population of lysosomes than does liver.…”

Section: Discussionmentioning

confidence: 99%

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Phosphodiesterase II in epithelial cells from guinea-pig and rat small intestine

Flanagan

Zbarsky

1974

Biochemical Journal

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Phosphodiesterase II activity was determined by using a synthetic substrate, the 2,4-dinitrophenyl ester of thymidine 3'-phosphate. The enzyme activity was determined in fractions obtained by differential centrifugation of homogenates of epithelial cells from the small intestinal mucosa of guinea pigs and rats. In guinea-pig preparations phosphodiesterase II occurred with highest specific activity in those fractions rich in succinate dehydrogenase and acid phosphatase. A lysosomal location for the guinea-pig enzyme was indicated by its structure-linked latency and by its association with particles that underwent a characteristic decrease in equilibrium density when Triton WR-1339 was injected into the animals. With rat preparations a much greater proportion of the phosphodiesterase II activity was found in the soluble fraction after ultracentrifugation. The rat enzyme exhibited a lower degree oflatency and administration of Triton WR-1 339 had no effect. The rat enzyme further differed from that of the guinea pig in other respects; it was more labile at 60°C, it exhibited a lower pH optimum and it had a higher molecular weight as determined by gel-filtration chromatography.

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Section: Discussionsupporting

confidence: 45%

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

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Phosphodiesterase II in epithelial cells from guinea-pig and rat small intestine

Flanagan

Zbarsky

1974

Biochemical Journal

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“…Experiments were performed with male and female Wistar rats weighing 200-300 g. Density+adient experiments were performed using a method similar to that of Beaufay et al [3]. Plasma membranes were isolated according to the method of Neville [4] with the modifications introduced by Emmelot et al [5].…”

Section: Methodsmentioning

confidence: 99%

Nucleoside diphosphatase in purified preparations of rat liver lysosomes

Coninck

Wattiaux

1969

FEBS Letters

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“…It is worth noting that the equilibrium position of mitochondria and lysosomes in sucrose gradients of rat liver tissue are within 0.02 g/ml of each other (BEAUFAY et al, 1964). On this basis, overlap of the mitochondrial and lysosomal distributions in these gradients would be expected.…”

Section: Density Gradient Analysis Of Acid Dnase and Dnase-j Activitymentioning

confidence: 99%

A subcellular localization of the gene product of the DNase-1 locus in Drosophila melanogaster

Detwiler

MacIntyre

1980

Insect Biochemistry

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Abstract-A study was undertaken to determine the subcellular location of DNase-I, a major acid deoxyribonuclease in Drosophila melanogaster. Embryonic tissue used in these experiments was derived from a wild type strain and from a strain homozygous at the DNase-l locus (3-61.8) for the null activity allele, DNase-lnl24. The majority of total acid DNase and DNase-l activity is found in the small particulate fraction of tissue homogenates fractionated by differential centrifugation. The activity exhibits latency in these extracts indicating that it is membrane delimited. DNase-I activity also co-equilibrates in sucrose density gradients with acid phosphatase activity which, in D. melanogaster, is known to be lysosomal. These results suggest that DNase-l is localized largely within the Iysosomes of embryonic tissue. Functional implications of a lysosomal location for DNase-l are discussed.

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Tissue fractionation studies. 18. Resolution of mitochondrial fractions from rat liver into three distinct populations of cytoplasmic particles by means of density equilibration in various gradients

Cited by 337 publications

References 15 publications

Phosphodiesterase II in epithelial cells from guinea-pig and rat small intestine

Phosphodiesterase II in epithelial cells from guinea-pig and rat small intestine

Nucleoside diphosphatase in purified preparations of rat liver lysosomes

A subcellular localization of the gene product of the DNase-1 locus in Drosophila melanogaster

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