Pig liver phosphomevalonate kinase. 1. Purification and properties

Sergio Bazaes, Enrique Beytía, Ana María Jabalquinto, Francisco Solís De Ovando, Isabel Gómez, Jaime Eyzaguirre

Resultado de la investigación: Article

20 Citas (Scopus)

Resumen

Pig liver phosphomevalonate kinase (EC 2.7.4.2) has been purified to homogeneity as shown by polyacrylamide gel electrophoresis. The molecular weight estimates range from 21 000 to 22 500. Each molecule is composed of one polypeptide chain. The presence of SH-containing reagents is essential for the preservation of enzyme activity at all steps in the purification. The enzyme shows absolute specificity for ATP and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 7.5 to over 9.5. Kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.075 mM and 0.46 mM have been obtained for phosphomevalonate and ATP, respectively. Amino acid composition shows a high content of acid amino acids, one cysteine residue per molecule of enzyme, and the absence of methionine. The results obtained suggest that the enzyme plays no regulatory function in cholesterol biosynthesis in pig liver, although a variable enzyme content was detected in different livers.

Idioma originalEnglish
Páginas (desde-hasta)2300-2304
Número de páginas5
PublicaciónBiochemistry
Volumen19
N.º11
EstadoPublished - 1980

Huella dactilar

Liver
Purification
Swine
Enzymes
Adenosine Triphosphate
Amino Acids
Molecules
Biosynthesis
Enzyme activity
Sulfhydryl Reagents
Electrophoresis
Methionine
Divalent Cations
Cysteine
Cations
Metals
Molecular weight
Cholesterol
phosphomevalonate kinase
Polyacrylamide Gel Electrophoresis

ASJC Scopus subject areas

  • Biochemistry

Citar esto

Bazaes, S., Beytía, E., Jabalquinto, A. M., Solís De Ovando, F., Gómez, I., & Eyzaguirre, J. (1980). Pig liver phosphomevalonate kinase. 1. Purification and properties. Biochemistry, 19(11), 2300-2304.
Bazaes, Sergio ; Beytía, Enrique ; Jabalquinto, Ana María ; Solís De Ovando, Francisco ; Gómez, Isabel ; Eyzaguirre, Jaime. / Pig liver phosphomevalonate kinase. 1. Purification and properties. En: Biochemistry. 1980 ; Vol. 19, N.º 11. pp. 2300-2304.
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Bazaes, S, Beytía, E, Jabalquinto, AM, Solís De Ovando, F, Gómez, I & Eyzaguirre, J 1980, 'Pig liver phosphomevalonate kinase. 1. Purification and properties', Biochemistry, vol. 19, n.º 11, pp. 2300-2304.

Pig liver phosphomevalonate kinase. 1. Purification and properties. / Bazaes, Sergio; Beytía, Enrique; Jabalquinto, Ana María; Solís De Ovando, Francisco; Gómez, Isabel; Eyzaguirre, Jaime.

En: Biochemistry, Vol. 19, N.º 11, 1980, p. 2300-2304.

Resultado de la investigación: Article

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T1 - Pig liver phosphomevalonate kinase. 1. Purification and properties

AU - Bazaes, Sergio

AU - Beytía, Enrique

AU - Jabalquinto, Ana María

AU - Solís De Ovando, Francisco

AU - Gómez, Isabel

AU - Eyzaguirre, Jaime

PY - 1980

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AB - Pig liver phosphomevalonate kinase (EC 2.7.4.2) has been purified to homogeneity as shown by polyacrylamide gel electrophoresis. The molecular weight estimates range from 21 000 to 22 500. Each molecule is composed of one polypeptide chain. The presence of SH-containing reagents is essential for the preservation of enzyme activity at all steps in the purification. The enzyme shows absolute specificity for ATP and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 7.5 to over 9.5. Kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.075 mM and 0.46 mM have been obtained for phosphomevalonate and ATP, respectively. Amino acid composition shows a high content of acid amino acids, one cysteine residue per molecule of enzyme, and the absence of methionine. The results obtained suggest that the enzyme plays no regulatory function in cholesterol biosynthesis in pig liver, although a variable enzyme content was detected in different livers.

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Bazaes S, Beytía E, Jabalquinto AM, Solís De Ovando F, Gómez I, Eyzaguirre J. Pig liver phosphomevalonate kinase. 1. Purification and properties. Biochemistry. 1980;19(11):2300-2304.