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Literature DB >> 3037402

Properties of the 3'-phosphoadenosine-5'-phosphosulfate (PAPS) synthesizing systems of brain and liver.

Abstract

Chromatography of brain and liver 100,000 g supernatants over HPLC molecular sieve columns revealed striking differences in the molecular weight distribution of ATP-sulfurylase and APS-kinase of the two tissues, pointing to different enzymic species for both enzymes in brain and liver. This was further substantiated by kinetic characterization of the two enzymes of both tissues. APS-kinase of liver is allosterically activated by ATP, while the brain enzyme is not. ATP-sulfurylase of brain is activated at high, but still physiological concentrations of ATP. Brain ATP-sulfurylase is inhibited by phenylalanine.

Entities: Chemical

Mesh：

Substances：

Year: 1987 PMID： 3037402 DOI： 10.1007/BF00993243

Source DB: PubMed Journal: Neurochem Res ISSN： 0364-3190 Impact factor: 3.996

15 in total

1. EFFECT OF ISCHEMIA ON KNOWN SUBSTRATES AND COFACTORS OF THE GLYCOLYTIC PATHWAY IN BRAIN.

Authors: O H LOWRY; J V PASSONNEAU; F X HASSELBERGER; D W SCHULZ
Journal: J Biol Chem Date: 1964-01 Impact factor: 5.157

2. Purification and properties of ATP-sulfurylase from Furth mouse mastocytoma.

Authors: M Shoyab; L Y Su; W Marx
Journal: Biochim Biophys Acta Date: 1972-01-20

3. Specific interaction of central nervous system myelin basic protein with lipids. Specific regions of the protein sequence protected from the proteolytic action of trypsin.

Authors: Y London; F G Vossenberg
Journal: Biochim Biophys Acta Date: 1973-05-25

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

Authors: A S Levi; G Wolf
Journal: Biochim Biophys Acta Date: 1969-04-22

5. The protection of A1 myelin basic protein against the action of proteolytic enzymes after interaction of the protein with lipids at the air-water interface.

Authors: Y London; R A Demel; W S Geurts van Kessel; F G Vossenberg; L L van Deenen
Journal: Biochim Biophys Acta Date: 1973-07-18

6. Enzyme-substrate complexes of ATP-sulfurylase from mouse mastocytoma.

Authors: M Shoyab; W Marx
Journal: Biochim Biophys Acta Date: 1972-01-20

7. Defect in 3'-phosphoadenosine 5'-phosphosulfate synthesis in brachymorphic mice. I. Characterization of the defect.

Authors: K Sugahara; N B Schwartz
Journal: Arch Biochem Biophys Date: 1982-04-01 Impact factor: 4.013

8. Defect in 3'-phosphoadenosine 5'-phosphosulfate synthesis in brachymorphic mice. II. Tissue distribution of the defect.

Authors: K Sugahara; N B Schwartz
Journal: Arch Biochem Biophys Date: 1982-04-01 Impact factor: 4.013

Properties of the 3'-phosphoadenosine-5'-phosphosulfate (PAPS) synthesizing systems of brain and liver.

1. EFFECT OF ISCHEMIA ON KNOWN SUBSTRATES AND COFACTORS OF THE GLYCOLYTIC PATHWAY IN BRAIN.

2. Purification and properties of ATP-sulfurylase from Furth mouse mastocytoma.

3. Specific interaction of central nervous system myelin basic protein with lipids. Specific regions of the protein sequence protected from the proteolytic action of trypsin.

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

5. The protection of A1 myelin basic protein against the action of proteolytic enzymes after interaction of the protein with lipids at the air-water interface.

6. Enzyme-substrate complexes of ATP-sulfurylase from mouse mastocytoma.

7. Defect in 3'-phosphoadenosine 5'-phosphosulfate synthesis in brachymorphic mice. I. Characterization of the defect.

8. Defect in 3'-phosphoadenosine 5'-phosphosulfate synthesis in brachymorphic mice. II. Tissue distribution of the defect.

9. Brain protein and myelin metabolism in hyperphenylalaninemic rats.

10. Effect of experimental hyperphenylalaninemia on myelin metabolism at later stages of brain development.

1. Kinetic mechanism of adenosine 5'-phosphosulphate kinase from rat chondrosarcoma.

2. Regional distribution of the phenylalanine-sensitive ATP-sulphurylase in brain.

3. The development of the muscarinic acetylcholine receptor in normal and hyperphenylalaninemic rat cerebrum.