Glucose-6-phosphatase

Baginski, Eugene S.; Foà, Piero P.; Zak, Bennie

doi:10.1016/b978-0-12-091302-2.50072-4

Cited by 191 publications

(92 citation statements)

References 18 publications

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“…The results reported in Table 1 clearly show that the ATPase activity of I-LN-DF~ in the presence of Fe(III) is very much lower than in the presence of Mg(II) and comparable to that observed in I-LN-DF t is suspended at 0.004/.tM in 50 mM Tris-HCl pH 8, 1.25 mM MgC12 and 2.5 mM ATE After 1-5 min, aliquots are withdrawn, added with 4% perchloric acid and centrifuged 10 min at 10,000 ×g. The supernatants are then used for the determination of inorganic phosphate as in [29]. When no metal or Fe(lII) is added to the assay mixture, I-LN-DF~ is 18 /,tM and ATP varies from 2.5 to 8 mM while Fe(III):ATP ratio is maintained 0.…”

Section: Fe(iii) Is a Poor Cojhctorjor Atp Hydrolysis Catalyzed Bymentioning

confidence: 99%

Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

et al. 1996

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Section: Fe(iii) Is a Poor Cojhctorjor Atp Hydrolysis Catalyzed Bymentioning

confidence: 99%

Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

et al. 1996

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“…The succinate dependent reduction of 2,6-dichloroindophenol was monitored at 600 nm. Glucose-6-phosphatase was assayed by the method of Baginski et al [18]. NADPH-cytochrome i. reductase was determined by the method of Phillips and Langdon [19].…”

Section: Assuysmentioning

confidence: 99%

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

Ilsbroux¹,

Vanduffel²,

Teuchy³

et al. 1985

European Journal of Biochemistry

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Basal‐lateral and brush border membranes from pig kidney cortex were prepared by differential centrifugation followed by free‐flow electrophoresis. In each type of membrane, azide‐insensitive, low‐affinity Ca2+‐ATPase and Mg2+‐ATPase activities are demonstrated. A comparative study for both membranes further reveals the following analogies between these ATPase: (a) they show maximal activity between pH 8 and 8.5; (b) they exhibit Km values for Ca‐ATP or Mg‐ATP in the millimolar range and have a comparable low substrate specificity; (c) they are insensitive to 10 μM of vanadate, N,N′‐dicyclohexylcarbodiimide, diethylstillbestrol, quercetin, harmaline and amiloride. The partial inhibition by 1 mM of the various compounds is rather aspecific. In view of these similarities it is concluded that only one enzyme entity is responsible for the activity which is measured in both membrane types. The HCO3−‐stimulated Mg2+‐ATPase activity in pig kidney cortex was also studied. This enzyme, however, is clearly of mitochondrial origin since the HCO3−‐stimulation coincides with the distribution profile of succinate dehydrogenase, a mitochondrial marker; and since it is inhibited by azide.

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“…Glucose-6-phosphatase (EC. 3.1.3.9) was determined according to the method of Baginsky et al (3). The phosphate liberated in the reaction was analyzed with the malachite green reaction (28).…”

Section: Methods and Materi-alsmentioning

confidence: 99%

γ-Glutamyltranspeptidase in the Rat Liver after Portacaval Shunt

et al. 1976

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Extractweight have been re~orted (I. 15). The metabolism of bile salts and y-Glutamyltranspeptidase (GGTP) activity was studied in livers of rats submitted to an end-to-side portacaval shunt (PCS) and in developing animals. To correlate the evolution of the enzymatic activity measured in vitro, histochemical techniques were used to localize enzyme activity in liver tissue. The GGTP activity in the adult rats was low and amounted to 2.0 =k 0.1 pmol/min/g. During fetal development the enzyme activity rose beginning on the 15th gestational day from 630 A 97 to 1,058 + 20 on the first postnatal day. I'hen the values declined and reached nearly adult values from the 10th postnatal day.After PCS the GGTP activity exhibited a three-to sixfold increase (130 + 69 to 371 + 131) as compared with uneperated adult controls (53 & 13). The highest levels corresponded to those observed between the 3rd and 5th postnatal day in the developing rats. The histochemistry of GGTP in the fetal and newborn liver showed a regular distribution of the enzyme as a fine deposit in the hepatocytes throughout the whole tissue. Ten days after birth the activity was low, at the same level as in the adult rat. In the period after P C S hepatocytes began to show signs of enzymatic activity at the periphery of the hepatic lobules, which subsequently spread through the whole lobules. The increase of GGTP activity after P C S equaled the activity found in fetal animals. That correlated well in both groups with the reappearance of histologically demonstrable enzyme activity in hepatocytes. SpeculationThe consequences of portacaval shunt might be associated with the derepression of an enzyme normally present only in fetal and neonatal rat liver. Since GGTP plays a role in the y-glutamyl cycle, and is responsible, supposedly, for the transport of amino acids into the cell, it may be that in fetal liver and after P C S augmented cellular amino acid transport is an expression of growth and transformation processes.The end-to-side PCS in the rat represents an appropriate model to study experimental hyperammonemia (7, 15) because of the shunting of portal blood to the systemic circulation. In addition to hyperammonemia, portacaval shunting leads to marked changes of the quantity and composition of the blood reaching the liver. The consequences of the shunt operation are therefore multiple. Encephalopathy, testicular atrophy, and changes in body and liver of certain amino ac'ids seeks to'be affected as well (14,(24)(25)(26).These significant morphologic and functional changes are likely to be interpreted as a consequence of shunt-induced alterations in the metabolic stimulation of the liver. Despite considerable work in this field, no common denominator has been found to define the underlying hepatic process of the transformations induced by PCS. To our knowledge the specific hypothesis has not been tested of whether some of the consequences of PCS on hepatic metabolism might be considered as a regression of the liver cell function to a more immature or embr...

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Glucose-6-phosphatase

Cited by 191 publications

References 18 publications

Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex

γ-Glutamyltranspeptidase in the Rat Liver after Portacaval Shunt

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Glucose-6-phosphatase

Cited by 191 publications

References 18 publications

Characterization of the binding of Fe(III) to F1ATPase from bovine heart mitochondria

Characterization of the binding of Fe(III) to F1ATPase from bovine heart mitochondria

An azide‐insensitive low‐affinity ATPase stimulated by Ca2+ or Mg2+ in basal‐lateral and brush border membranes of kidney cortex

γ-Glutamyltranspeptidase in the Rat Liver after Portacaval Shunt

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Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

Characterization of the binding of Fe(III) to F₁ATPase from bovine heart mitochondria

An azide‐insensitive low‐affinity ATPase stimulated by Ca²⁺ or Mg²⁺ in basal‐lateral and brush border membranes of kidney cortex