Isolation of rat-liver lysosomes and their general properties

Sawant, P. L.; Shibko, S.; Kumta, U.S.; Tappel, Al L.

doi:10.1016/0926-6569(64)90169-5

Cited by 93 publications

(59 citation statements)

References 16 publications

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“…For complex I, a commercial preparation (Platinol, Bristol) was also employed. Lysosome-enriched preparations were obtained according to [16], except that purification was arrested at step II (fraction II). Depending perhaps on the criterion adopted for pellet removal after centrifugation at 16 500 × g, variable increase (10-18-times, aver-…”

Section: Methodsmentioning

confidence: 99%

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

Antone

1982

FEBS Letters

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Section: Methodsmentioning

confidence: 99%

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

Antone

1982

FEBS Letters

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“…25 M sucrose, and washed several times with the same medium. Lysosomes, for which data are presented in Tables 1-3, were purified according to the procedure of Sawant et al [19].…”

Section: Methodsmentioning

confidence: 99%

Intracellular Localization of Phosphodiesterases I and II in Rat Liver

Erecińska

Sierakowska

Shugar

1969

European Journal of Biochemistry

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Differential and density gradient centrifugation techniques have been employed to study the intracellular distribution of phosphodiesterases I and I1 in rat liver, using as specific substrates the p-nitrophenyl esters of thymidine-5'-phosphate and thymidine-3'-phosphate. Some of the results for phosphodiesterase I were also examined with the use of a 5'-terminated DNA core as substrate.Phosphodiesterase I was found to be largely (> 80°/,) localized in the plasma membrane, whereas purified nuclei, rough microsomes, and the inner mitochondria1 membrane are essentially free of this enzyme. The possible sources of apparent phosphodiesterase I activity of the outer mitochondrial membrane, the lysosomes and the smooth microsomal membrane are discussed.Phosphodiesterase I1 is localized largely in the soluble fraction of the lysosomes, and exhibits the latency typical of lysosomal hydrolases. The overall findings are examined in relation to those of other investigators. Possible reservations regarding the absolute specificities of the substrates employed, and their bearing on the localization results, are discussed.The delineation of the specificities of phosphodiesterases I and I1 [1,2], and the preparation o f relatively specific and convenient substrates for the assay of these enzymes [3-61, has paved the way for studies on their intracellular distribution [S].With p-nitrophenyl thymidine-5'-phosphate as substrate, Razzell [7] first demonstrated the localization of phosphodiesterase I largely in the microsomal fraction of rat liver. Subsequently deLamirande et al. [8,9] reported the presence of bhe enzyme in the nuclei and the microsomal membranes, and the absence of any activity in the ribosomes. The microsoma1 localization of phosphodiesterase I was subsequently supported by Brightwell and Tappel [lo]. On the other hand, cytochemical investigations on phosphodiesterase I localization in rat liver, with the aid of cc-napht*hyl thymidine-5'-phosphate as substrate, revealed most of the enzyme activity a t the border of the bile canaliculi [4].

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“…Rat liver lysosomes were prepared according to Sawant et al [19] and resuspended before use at 0 8C in a medium (mother solution) containing 0.25 M sucrose, 10 mM Mops-Hepes pH 7.4 and 5 mM MgSO 4 . Acridine Orange (AO) (Merck) was purified according to Pal and Schubert [20].…”

Section: Methodsmentioning

confidence: 99%

The interaction of methylmercury with lysosomes from rat liver

Bragadin

Scutari

Manente

et al. 2002

Inorganica Chimica Acta

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The interactions of methylmercury with rat liver lysosomes were investigated. The results indicate that methylmercury enhances the proton permeability in membranes. Since this uncoupling mechanism necessarily implies the transport of a charged ion (in this case CH 3 Hg ' ) through the membrane, this fact can help to explain why a preferential target of methylmercury are nerve cells, whose plasma membrane potential has the highest value, when compared with other cells. #

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Isolation of rat-liver lysosomes and their general properties

Cited by 93 publications

References 16 publications

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

Intracellular Localization of Phosphodiesterases I and II in Rat Liver

The interaction of methylmercury with lysosomes from rat liver

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