Purification and properties of two adenosine-5′-phosphosulphate sulphohydrolases from rat liver and their possible role in the degradation of 3′-phosphoadenosine 5′-phosphosulphate
- 11 November 1970
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 220 (2) , 284-299
- https://doi.org/10.1016/0005-2744(70)90013-6
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Subcellular distribution of two enzyme systems which degrade 3′-phosphoadenosine 5′-phosphosulfate (“Active sulfate”)Biochimica et Biophysica Acta (BBA) - General Subjects, 1969
- Synthesis and degradation of active sulfate in liverBiochimica et Biophysica Acta (BBA) - General Subjects, 1969
- Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin ABiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- A rat liver sulphohydrolase enzyme acting on adenylyl sulphateBiochemical Journal, 1969
- BIOSYNTHESIS OF l-TYROSINE O-SULPHATE FROM THE METHYL AND ETHYL ESTERS OF l-TYROSINEBiochemical Journal, 1965
- Enzymic degradation of active sulphateBiochimica et Biophysica Acta, 1962
- Determination of inorganic sulphate in studies on the enzymic and non-enzymic hydrolysis of carbohydrate and other sulphate estersBiochemical Journal, 1961
- Endogenous sulphate acceptors in rat liverBiochemical Journal, 1960
- Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissueBiochemical Journal, 1955
- Tissue fractionation studies. 4. Comparative study of the binding of acid phosphatase, β-glucuronidase and cathepsin by rat-liver particlesBiochemical Journal, 1955