EsturgeonV1, Istex, Corpus, bibRecord, 000809

Kinetic properties of liver pyruvate kinase from the flounder ( Platichthys flesus L.)

Identifieur interne : 000809 ( Istex/Corpus ); précédent : 000808; suivant : 000810

Kinetic properties of liver pyruvate kinase from the flounder ( Platichthys flesus L.)

Auteurs : Ole Sand

Source :

Comparative Biochemistry and Physiology, Part B: Biochemistry and Molecular Biology [ 0305-0491 ] ; 1986.

RBID : ISTEX:15CA570E02C132187AB3DA79A08CC479B003ADEB

Abstract

1.1. Pyruvate kinase, purified from flounder liver, in two forms, i.e. PK I and PK II, is characterized by sigmoid kinetics with phosphoenolpyruvate as substrate at pH 6.3, 6.7 and 7.7.2.2. K0.5 for PEP increases with increasing pH.3.3. PK I and PK II show hyperbolic kinetics with ADP, but are inhibited by ADP concentrations above 1–2 mM.4.4. K0.5 for ADP decreases with increasing pH.5.5. PK I and PK II differ in their K0.5 values for PEP with a factor of at least 2, showing the highest figures for the latter. K0.5 for ADP is about the same for the two enzyme forms.6.6. Other nucleoside diphosphates can replace ADP as the substrate.7.7. When the nucleoside diphosphates are arranged in a rank order showing decreasing effectiveness as substrate, different rank orders are obtained for PK I and PK II.

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https://api.istex.fr/document/15CA570E02C132187AB3DA79A08CC479B003ADEB/fulltext/pdf

DOI: 10.1016/0305-0491(86)90276-2

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ISTEX:15CA570E02C132187AB3DA79A08CC479B003ADEB

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<front><div type="abstract" xml:lang="en">1.1. Pyruvate kinase, purified from flounder liver, in two forms, i.e. PK I and PK II, is characterized by sigmoid kinetics with phosphoenolpyruvate as substrate at pH 6.3, 6.7 and 7.7.2.2. K0.5 for PEP increases with increasing pH.3.3. PK I and PK II show hyperbolic kinetics with ADP, but are inhibited by ADP concentrations above 1–2 mM.4.4. K0.5 for ADP decreases with increasing pH.5.5. PK I and PK II differ in their K0.5 values for PEP with a factor of at least 2, showing the highest figures for the latter. K0.5 for ADP is about the same for the two enzyme forms.6.6. Other nucleoside diphosphates can replace ADP as the substrate.7.7. When the nucleoside diphosphates are arranged in a rank order showing decreasing effectiveness as substrate, different rank orders are obtained for PK I and PK II.</div>
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<abstract>1.1. Pyruvate kinase, purified from flounder liver, in two forms, i.e. PK I and PK II, is characterized by sigmoid kinetics with phosphoenolpyruvate as substrate at pH 6.3, 6.7 and 7.7.2.2. K0.5 for PEP increases with increasing pH.3.3. PK I and PK II show hyperbolic kinetics with ADP, but are inhibited by ADP concentrations above 1–2 mM.4.4. K0.5 for ADP decreases with increasing pH.5.5. PK I and PK II differ in their K0.5 values for PEP with a factor of at least 2, showing the highest figures for the latter. K0.5 for ADP is about the same for the two enzyme forms.6.6. Other nucleoside diphosphates can replace ADP as the substrate.7.7. When the nucleoside diphosphates are arranged in a rank order showing decreasing effectiveness as substrate, different rank orders are obtained for PK I and PK II.</abstract>
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<head><ce:dochead><ce:textfn>General paper</ce:textfn>
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<ce:title>Kinetic properties of liver pyruvate kinase from the flounder (<ce:italic>Platichthys flesus</ce:italic>
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<ce:para>1. Pyruvate kinase, purified from flounder liver, in two forms, i.e. PK I and PK II, is characterized by sigmoid kinetics with phosphoenolpyruvate as substrate at pH 6.3, 6.7 and 7.7.</ce:para>
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<ce:para>3. PK I and PK II show hyperbolic kinetics with ADP, but are inhibited by ADP concentrations above 1–2 mM.</ce:para>
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<ce:list-item><ce:label>5.</ce:label>
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<ce:para>6. Other nucleoside diphosphates can replace ADP as the substrate.</ce:para>
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<ce:para>7. When the nucleoside diphosphates are arranged in a rank order showing decreasing effectiveness as substrate, different rank orders are obtained for PK I and PK II.</ce:para>
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<abstract lang="en">1.1. Pyruvate kinase, purified from flounder liver, in two forms, i.e. PK I and PK II, is characterized by sigmoid kinetics with phosphoenolpyruvate as substrate at pH 6.3, 6.7 and 7.7.2.2. K0.5 for PEP increases with increasing pH.3.3. PK I and PK II show hyperbolic kinetics with ADP, but are inhibited by ADP concentrations above 1–2 mM.4.4. K0.5 for ADP decreases with increasing pH.5.5. PK I and PK II differ in their K0.5 values for PEP with a factor of at least 2, showing the highest figures for the latter. K0.5 for ADP is about the same for the two enzyme forms.6.6. Other nucleoside diphosphates can replace ADP as the substrate.7.7. When the nucleoside diphosphates are arranged in a rank order showing decreasing effectiveness as substrate, different rank orders are obtained for PK I and PK II.</abstract>
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Kinetic properties of liver pyruvate kinase from the flounder ( Platichthys flesus L.)

Kinetic properties of liver pyruvate kinase from the flounder ( Platichthys flesus L.)

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Abstract

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Pour manipuler ce document sous Unix (Dilib)

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