Acid phosphatase of the lysosomal and soluble fraction of rat liver

Shibko, S.; Tappel, Al L.

doi:10.1016/0926-6569(63)90110-x

Cited by 136 publications

(24 citation statements)

References 17 publications

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“…Among inorganic compounds, NaF was found to reduce by 50% the FAD hydrolysis reaction rate at 1 mM; at higher concentrations, NaF strongly inhibited the reaction. No inhibition was found by tartrate (used at concentrations up to 1 mM), a powerful inhibitor of the lysosomal acid phosphatase (48).…”

Section: Resultsmentioning

confidence: 99%

FAD Synthesis and Degradation in the Nucleus Create a Local Flavin Cofactor Pool

Giancaspero

Busco

Panebianco

et al. 2013

Journal of Biological Chemistry

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Background: FAD synthase is known to catalyze the biosynthesis of FAD in cytosol and mitochondria. Results: The existence of a nuclear FAD synthase and a FAD-hydrolyzing activity is demonstrated. Conclusion: A dynamic pool of FAD exists in the nucleus. Significance: Nuclear, mitochondrial, and cytosolic FAD synthase pools constitute a flavin network involved in the regulation of cellular metabolism and epigenetic events.

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Section: Resultsmentioning

confidence: 99%

FAD Synthesis and Degradation in the Nucleus Create a Local Flavin Cofactor Pool

Giancaspero

Busco

Panebianco

et al. 2013

Journal of Biological Chemistry

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“…Other compounds, including dithiothreitol, EDTA and o-phenanthroline (1 mM each) can inhibit both mitochondrial and lysosomal enzymes, whereas externally added Mg2+ (1 mM) and Zn2+ (0.1 mM) were found to stimulate mitochondrial FAD pyrophosphatase (60% and 200% increase, respectively) with 10 pM FAD used as a substrate, but have no significant effect on lysosomal FAD pyrophosphatase. L-Tartrate (5 mM), a powerful inhibitor of the acid phosphatase (Shibko and Tappel, 1963), fails to inhibit mitochondrial FAD pyrophosphatase and mitochondrial FMN phosphohydrolase, when 1 5 p M FAD and 2 m M FMN were used as substrates.…”

Section: Resultsmentioning

confidence: 99%

“…1 (seven experiments). The lysosomal contamination in purified RLM was checked by measuring the activities of the acid FAD pyrophosphatase and acid phosphatase, lysosomal enzymes associated with soluble fraction and both soluble and membrane fractions, respectively (Ragab et al, 1968 ;Shibko and Tappel, 1963). Acid FAD pyrophosphatase activity could not be detected in purified RLM, while the acid phosphatase specific activity was found to decrease by 90 2 7 % (five experiments) compared to that found in non-purified mitochondria.…”

Section: Methodsmentioning

confidence: 99%

Flavin Adenine Dinucleotide and Flavin Mononucleotide Metabolism in Rat Liver

Barile¹,

Brizio²,

Virgilio³

et al. 1997

European Journal of Biochemistry

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In order to gain some insight into mitochondrial flavin biochemistry, rat liver mitochondria essentially free of lysosomal and microsomal contamination were prepared and their capability to metabolise externally added and endogenous FAD and FMN tested both spectroscopically and via HPLC.The existence of two novel mitochondrial enzymes, namely FAD pyrophosphatase (EC 3.6.1.18) and FMN phosphohydrolase (EC 3.1.3.2), which catalyse FAD+FMN and FMN-riboflavin conversion, respectively, is shown. They differ from each other and from extramitochondrial enzymes, as judged by their pH profile and inhibitor sensitivity, and can be separated in a partial FAD pyrophosphatase purification.Digitonin titration and subfractionation experiments show that FAD pyrophosphatase is located in the outer mitochondrial membrane and FMN phosphohydrolase in the intermembrane space. Since these enzymes can metabolise endogenous FAD and FMN, which are made available by using both Triton X-100 and the effector oxaloacetate, a proposal is made that FAD pyrophosphatase and FMN phosphohydrolase play a major role in mitochondrial flavoprotein turnover.

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“…Mitochondrial separation was estimated by cytochrome oxidase activity with cytochrome c and N,N-dimethyl-p-phenylenediamine (10). Lysosomal separation was evaluated by acid phosphatase activity with p-nitrophenyl phosphate (11). Portions were exposed to 0.5% Triton in glycine buffer pH 4.5 containing 0.1 M alloxan to inactivate selectively free acid phosphatase activity (12).…”

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confidence: 99%

Hepatic intracellular distribution of tritium-labeled unconjugated and conjugated bilirubin in normal and Gunn rats.

Bernstein¹,

Ezzer²,

Gartner³

et al. 1966

J. Clin. Invest.

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Relatively little is known about the mechanism, regulation, or subcellular localization of the hepatic uptake, storage, conjugation, and excretion of bilirubin. In the work here reported, the ultrastructural localization of the sites of these processes was studied by determining the subcellular distribution and chemical nature of bilirubin after the injection of physiologic amounts of tritiumlabeled unconjugated bilirubin (UCB-3H) and conjugated bilirubin (CB-3H) in normal and glucuronyl transferase-deficient (Gunn) rats (1, 2). Studies were also performed using bilirubin-14C for comparison with the intracellular distribution of tritiated bilirubin. While these studies were in progress, Brown, Grodsky, and Carbone (3) described the subcellular distribution of injected UCB-3H in normal rat liver. MethodsTritium-labeled bilirubin was prepared by the Wilzbach procedure and purified and equilibrated with crystalline bovine albumin to constant specific activity as described by Grodsky, Carbone, Fanska, and Peng (4). The purity of labeled bilirubin was established by diazotization, chro-* Submitted for publication January 28, 1966; accepted April 5, 1966. These studies were supported by research grants from the U. S. Public Health Service (AM 02019 and TI AM 5384) and the New York Heart Association and Heart Fund, Inc.This work was presented in part at the Eastern Sec- Bile obtained from normal rats injected with UCB-'H was stored at -200 C for not more than 48 hours before use and served as a source of CB-8H. Chromatography and subsequent strip scanning of azo pigments obtained from this bile revealed 82 to 96% of the total radioactivity in bile to migrate with the conjugated azo pigment (Azo-B) on paper chromatograms. The mean specific activity of CB-'H was 60% of UCB-'H, and accordingly 85 to 125 ucg containing 1.5 X 107 dpm was used in each experiment.Bilirubin-'4C was prepared according to the technique of Ostrow, Hammaker, and Schmid (6) and was recrystallized to a constant specific activity of 0.91 mc per mmole.At intervals of 1 to 60 minutes after injection of UCB-8H, UCB-14C, or CB-'H, a single lobe of the liver was removed, maintained at 00 C, rinsed in 0.25 M sucrose at pH 7.4, blotted dry, weighed, and homogenized in a Teflon glass homogenizer containing 9.0 vol of the buffered sucrose solution. The order in which lobes were removed was varied in initial experiments, but no significant difference in uptake of radiobilirubin among different lobes was observed.Eight normal rats were injected with UCB-8H, and total intrahepatic radioactivity was estimated in homogenates of liver obtained at 1, 2,4,8,9,15, 30, 45, and 60 minutes after injection. Twenty studies of the subcellular distribution of radiobilirubin were performed using liver obtained from these rats at intervals from 1 to 60 minutes after injection of UCB-3H. Three normal 1194 HEPATIC DISTRIBUTION OF BILIRUBIN TABLE I

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Acid phosphatase of the lysosomal and soluble fraction of rat liver

Cited by 136 publications

References 17 publications

FAD Synthesis and Degradation in the Nucleus Create a Local Flavin Cofactor Pool

FAD Synthesis and Degradation in the Nucleus Create a Local Flavin Cofactor Pool

Flavin Adenine Dinucleotide and Flavin Mononucleotide Metabolism in Rat Liver

Hepatic intracellular distribution of tritium-labeled unconjugated and conjugated bilirubin in normal and Gunn rats.

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