Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver
Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in th...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1983 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular - Amsterdam : Elsevier, 749(1983), 3, Seite 329-332 |
| Übergeordnetes Werk: |
volume:749 ; year:1983 ; number:3 ; pages:329-332 |
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NLEJ186894279 |
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| 520 | |a Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. | ||
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(DE-627)NLEJ186894279 (DE-599)GBVNLZ186894279 DE-627 ger DE-627 rakwb eng Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Persat, F. oth Azzar, G. oth Martel, M.-B. oth Got, R. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 749(1983), 3, Seite 329-332 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:749 year:1983 number:3 pages:329-332 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 749 1983 3 329-332 |
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(DE-627)NLEJ186894279 (DE-599)GBVNLZ186894279 DE-627 ger DE-627 rakwb eng Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Persat, F. oth Azzar, G. oth Martel, M.-B. oth Got, R. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 749(1983), 3, Seite 329-332 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:749 year:1983 number:3 pages:329-332 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 749 1983 3 329-332 |
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(DE-627)NLEJ186894279 (DE-599)GBVNLZ186894279 DE-627 ger DE-627 rakwb eng Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Persat, F. oth Azzar, G. oth Martel, M.-B. oth Got, R. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 749(1983), 3, Seite 329-332 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:749 year:1983 number:3 pages:329-332 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 749 1983 3 329-332 |
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(DE-627)NLEJ186894279 (DE-599)GBVNLZ186894279 DE-627 ger DE-627 rakwb eng Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Persat, F. oth Azzar, G. oth Martel, M.-B. oth Got, R. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 749(1983), 3, Seite 329-332 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:749 year:1983 number:3 pages:329-332 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 749 1983 3 329-332 |
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(DE-627)NLEJ186894279 (DE-599)GBVNLZ186894279 DE-627 ger DE-627 rakwb eng Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Persat, F. oth Azzar, G. oth Martel, M.-B. oth Got, R. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 749(1983), 3, Seite 329-332 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:749 year:1983 number:3 pages:329-332 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 749 1983 3 329-332 |
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properties of uridine diphosphate glucose pyrophosphorylase from golgi apparatus of liver |
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Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver |
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Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. |
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Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. |
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Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186894279</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707062142.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1983 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186894279</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186894279</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Properties of uridine diphosphate glucose pyrophosphorylase from Golgi apparatus of liver</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1983</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Golgi apparatus isolated from cat liver contained UDPglucose pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9) activity. The results of washing suggested that pyrophosphorylase was bound firmly to Golgi membranes. Moreover, the enzyme was activated by Triton X-100 in the same extent as galactosyltransferase, a typical Golgi apparatus enzyme. Two-substrate kinetic studies were performed with the enzymes from cytosol and Golgi fractions. The soluble enzyme showed an apparent 2.5-fold greater activity for the glucose 1-phosphate than for UTP, while pyrophosphorylase of Golgi apparatus had the same affinity for the two substrates. A random mechanism was observed with a direct dependence of apparent Michaelis constant values on the concentration of second substrate for soluble enzyme. In contrast, with Golgi enzyme one ligand had no effect on the binding of the other.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Persat, F.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Azzar, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Martel, M.-B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Got, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">749(1983), 3, Seite 329-332</subfield><subfield code="w">(DE-627)NLEJ185338283</subfield><subfield code="w">(DE-600)2209539-1</subfield><subfield code="x">0167-4838</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:749</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:329-332</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90243-1</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">749</subfield><subfield code="j">1983</subfield><subfield code="e">3</subfield><subfield code="h">329-332</subfield></datafield></record></collection>
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7.400488 |