Isolation and sequence determination of an active site peptide of rabbit muscle pyruvate kinase

Guillermo Bezares, Jaime Eyzaguirre, Maria Victoria Hinrichs, Robert L. Heinrikson, Ilene Reardon, Robert G. Kemp, Steven P. Latshaw, Sergio Bazaes

Resultado de la investigación: Article

17 Citas (Scopus)

Resumen

Rabbit muscle pyruvate kinase was inactivated by 2′,3′-dialdehyde ADP with the incorporation of one molecule of reagent per enzyme subunit. The inactivated protein was digested with trypsin after reduction and carboxymethylation. The labeled peptide was isolated by gel filtration and further purified by HPLC. The peptide was sequenced both by liquid-phase and gas-phase automatic Edman degradation. A 34-residue peptide was obtained. This peptide is identical to a tryptic peptide labeled with trinitrobenze-nesulfonate, isolated and sequenced by Johnson et al. (Biochem. Biophys. Res. Commun. (1979) 90, 525-530) from bovine muscle pyruvate kinase. Available evidence suggests that dialdehyde ADP labels the enzyme at the same lysine in position 25 of the peptide, as found by Johnson et al. The high homology between the isolated peptide and regions of other pyruvate kinases from low to high eukaryotes supports the idea that this peptide is related to the enzyme active site.

Idioma originalEnglish
Páginas (desde-hasta)133-137
Número de páginas5
PublicaciónArchives of Biochemistry and Biophysics
Volumen253
N.º1
DOI
EstadoPublished - 15 feb 1987

Huella dactilar

Pyruvate Kinase
Sequence Analysis
Muscle
Catalytic Domain
Rabbits
Muscles
Peptides
Enzymes
Eukaryota
Trypsin
Lysine
Gel Chromatography
Labels
Gases
Gels
High Pressure Liquid Chromatography
Degradation
Molecules
Liquids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Citar esto

Bezares, Guillermo ; Eyzaguirre, Jaime ; Hinrichs, Maria Victoria ; Heinrikson, Robert L. ; Reardon, Ilene ; Kemp, Robert G. ; Latshaw, Steven P. ; Bazaes, Sergio. / Isolation and sequence determination of an active site peptide of rabbit muscle pyruvate kinase. En: Archives of Biochemistry and Biophysics. 1987 ; Vol. 253, N.º 1. pp. 133-137.
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abstract = "Rabbit muscle pyruvate kinase was inactivated by 2′,3′-dialdehyde ADP with the incorporation of one molecule of reagent per enzyme subunit. The inactivated protein was digested with trypsin after reduction and carboxymethylation. The labeled peptide was isolated by gel filtration and further purified by HPLC. The peptide was sequenced both by liquid-phase and gas-phase automatic Edman degradation. A 34-residue peptide was obtained. This peptide is identical to a tryptic peptide labeled with trinitrobenze-nesulfonate, isolated and sequenced by Johnson et al. (Biochem. Biophys. Res. Commun. (1979) 90, 525-530) from bovine muscle pyruvate kinase. Available evidence suggests that dialdehyde ADP labels the enzyme at the same lysine in position 25 of the peptide, as found by Johnson et al. The high homology between the isolated peptide and regions of other pyruvate kinases from low to high eukaryotes supports the idea that this peptide is related to the enzyme active site.",
author = "Guillermo Bezares and Jaime Eyzaguirre and Hinrichs, {Maria Victoria} and Heinrikson, {Robert L.} and Ilene Reardon and Kemp, {Robert G.} and Latshaw, {Steven P.} and Sergio Bazaes",
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Bezares, G, Eyzaguirre, J, Hinrichs, MV, Heinrikson, RL, Reardon, I, Kemp, RG, Latshaw, SP & Bazaes, S 1987, 'Isolation and sequence determination of an active site peptide of rabbit muscle pyruvate kinase', Archives of Biochemistry and Biophysics, vol. 253, n.º 1, pp. 133-137. https://doi.org/10.1016/0003-9861(87)90645-X

Isolation and sequence determination of an active site peptide of rabbit muscle pyruvate kinase. / Bezares, Guillermo; Eyzaguirre, Jaime; Hinrichs, Maria Victoria; Heinrikson, Robert L.; Reardon, Ilene; Kemp, Robert G.; Latshaw, Steven P.; Bazaes, Sergio.

En: Archives of Biochemistry and Biophysics, Vol. 253, N.º 1, 15.02.1987, p. 133-137.

Resultado de la investigación: Article

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AU - Bezares, Guillermo

AU - Eyzaguirre, Jaime

AU - Hinrichs, Maria Victoria

AU - Heinrikson, Robert L.

AU - Reardon, Ilene

AU - Kemp, Robert G.

AU - Latshaw, Steven P.

AU - Bazaes, Sergio

PY - 1987/2/15

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AB - Rabbit muscle pyruvate kinase was inactivated by 2′,3′-dialdehyde ADP with the incorporation of one molecule of reagent per enzyme subunit. The inactivated protein was digested with trypsin after reduction and carboxymethylation. The labeled peptide was isolated by gel filtration and further purified by HPLC. The peptide was sequenced both by liquid-phase and gas-phase automatic Edman degradation. A 34-residue peptide was obtained. This peptide is identical to a tryptic peptide labeled with trinitrobenze-nesulfonate, isolated and sequenced by Johnson et al. (Biochem. Biophys. Res. Commun. (1979) 90, 525-530) from bovine muscle pyruvate kinase. Available evidence suggests that dialdehyde ADP labels the enzyme at the same lysine in position 25 of the peptide, as found by Johnson et al. The high homology between the isolated peptide and regions of other pyruvate kinases from low to high eukaryotes supports the idea that this peptide is related to the enzyme active site.

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