Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin A.

@article{Levi1969PurificationAP,
  title={Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin A.},
  author={Arrigo Levi and George Wolf},
  journal={Biochimica et biophysica acta},
  year={1969},
  volume={178 2},
  pages={
          262-82
        }
}
  • A. LeviG. Wolf
  • Published 22 April 1969
  • Biology
  • Biochimica et biophysica acta
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44 Citations
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44 Citations

ATP-Sulfurylase From Penicillivm Chbysogenum. I. Purification and Characterization

A purified ATP-sulfurylase from Peniaillium ehrysogenum has been purified 945-fold by a procedure involving heat treatment, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration, with overall recovery of activity 47%.

Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions.

Adenosine 5'-triphosphate-sulfurylase in corn roots and its partial purification.

The data suggest that at least the first reaction in sulfate reduction might proceed as effectively in roots as in shoots, and in the presence of exogenous pyrophosphatase, the enzyme from roots exhibited specific activities as high as those obtained with the leaf enzyme.

Purification and properties of two forms of ATP sulfurylase from Euglena.

Purification and properties of ATP-sulphurylase from Nitrobacter agilis.

Purification and some properties of ATP-sulfurylase from developing sea urchin embryos.

  • A. Nozawa
  • Biology, Chemistry
    Biochimica et biophysica acta
  • 1980

Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate‐reducer, Archaeoglobus fulgidus

ATP sulfurylase (sulfate adenylyltransferase, EC 2.7.7.4) was isolated from the recently described extremely thermophilic sulfate-reducing archaebacterium Archaeglobus fulgidus. The enzyme was…

Purification and properties of the ATP sulphurylase of rat liver.

Adenosine triphosphate sulfurylase from Penicillium chrysogenum equilibrium binding, substrate hydrolysis, and isotope exchange studies.

Species specific release of sulfate from adenylyl sulfate by ATP sulfurylase or ADP sulfurylase in the green sulfur bacteria Chlorobium limicola and Chlorobium vibrioforme

High activities of ATP sulfurylase were found in the soluble protein fraction of two Chlorobium limicola strains, whereas ADP sulfuryLase was absent, and the stoichiometry of the reaction was proven.

References

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Vitamin A and the sulfate-activating enzymes.

METABOLIC REGULATION OF ADENOSINE TRIPHOSPHATE SULFURYLASE IN YEAST

The sulfate-reducing pathway in yeast appears to be regulated at its first step both by feedback inhibition (by sulfide) and by repression (by methionine).

The synthesis of 3'-phosphoadenosine 5'-phosphosulfate by retinae and livers of normal and vitamin A-deficient rats.

Enzymatic synthesis of adenosine-5'-phosphosulfate.

Biosynthesis of heparin. Separation of subcellular mastocytoma fractions involved in the incorporation of sulfate-35S into the heparin fraction.

Enzymatic reactions involving sulfate, sulfite, selenate, and molybdate.

The effect of vitamin A and other dietary constituents on the activity of adenosine triphosphate sulphurylase.

It is concluded that, when the effect of protein deprivation on ATP sulphurylase is separated from theeffect of vitamin A deficiency, a lowering of the enzyme activity caused by the vitamin deficiency is demonstrable.

Studies on metabolism of vitamin A. 2. Enzymic synthesis and hydrolysis of phenolic sulphates in vitamin-A-deficient rats.

It is shown here that in vitamin-A-deficient rats there is a slight increase in the urinary excretion of inorganic sulphate, whereas that of the ethereal sulphates is markedly reduced, and the activity of enzymes responsible for the sulphurylation of phenols is markedly lowered in the tissues of the deficient rats.

Rapid determination of picomole quantities of ATP with a liquid scintillation counter.

Purification of the hyperglycemic-glycogenolytic factor from insulin and from gastric mucosa.