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Three aspartate kinase isoenzymes from maize.

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Three aspartate kinase isoenzymes from maize. / Azevedo, R. A.; Blackwell, R. D.; Smith, R. J. et al.
In: Phytochemistry, Vol. 31, No. 11, 1992, p. 3725-3730.

Research output: Contribution to Journal/Magazine › Journal article

Harvard

Azevedo, RA, Blackwell, RD, Smith, RJ & Lea, PJ 1992, 'Three aspartate kinase isoenzymes from maize.', Phytochemistry, vol. 31, no. 11, pp. 3725-3730. https://doi.org/10.1016/S0031-9422(00)97516-2

APA

Azevedo, R. A., Blackwell, R. D., Smith, R. J., & Lea, P. J. (1992). Three aspartate kinase isoenzymes from maize. Phytochemistry, 31(11), 3725-3730. https://doi.org/10.1016/S0031-9422(00)97516-2

Vancouver

Azevedo RA, Blackwell RD, Smith RJ, Lea PJ. Three aspartate kinase isoenzymes from maize. Phytochemistry. 1992;31(11):3725-3730. doi: 10.1016/S0031-9422(00)97516-2

Author

Azevedo, R. A. ; Blackwell, R. D. ; Smith, R. J. et al. / Three aspartate kinase isoenzymes from maize. In: Phytochemistry. 1992 ; Vol. 31, No. 11. pp. 3725-3730.

Bibtex

@article{9992830bef37424e810f10164a93cda3,
title = "Three aspartate kinase isoenzymes from maize.",
abstract = "Aspartate kinase was purified from maize cells to near homogeneity after five steps of purification including ammonium sulphate, anion exchange chromatography, gel filtration and polyacrylamide gel electrophoresis. Two peaks of aspartate kinase activity could be eluted from anion exchange chromatography columns (Fast Flow Q Sepharose and Mono Q HR 5/5) with 150 and 200 mM KCl. Both peaks showed sensitivity to -lysine and the second peak in elution order was also inhibited by S-adenosylmethionine alone. Gels stained for aspartate kinase activity showed one broad band sensitive to inhibition by lysine. This band was electroeluted from the gel and further analysis showed the presence of three protein bands. The least electronegative band on the gel was identified as aspartate kinase. A third form of aspartate kinase, inhibited by threonine, was identified by gel filtration. The native Mr of the two lysine-sensitive forms of the enzyme was ca 150 000 and the threonine-sensitive enzyme 180 000, values different from those previously reported. These results confirm the hypothesis that in higher plants, at least three isoenzymic forms of aspartate kinase are present, two sensitive to lysine, the other to threonine.",
keywords = "Zea mays, aspartate kinase, lysine, threonine, S-adenosyhnethionine.",
author = "Azevedo, {R. A.} and Blackwell, {R. D.} and Smith, {R. J.} and Lea, {P. J.}",
year = "1992",
doi = "10.1016/S0031-9422(00)97516-2",
language = "English",
volume = "31",
pages = "3725--3730",
journal = "Phytochemistry",
publisher = "Elsevier Limited",
number = "11",

}

RIS

TY - JOUR

T1 - Three aspartate kinase isoenzymes from maize.

AU - Azevedo, R. A.

AU - Blackwell, R. D.

AU - Smith, R. J.

AU - Lea, P. J.

PY - 1992

Y1 - 1992

N2 - Aspartate kinase was purified from maize cells to near homogeneity after five steps of purification including ammonium sulphate, anion exchange chromatography, gel filtration and polyacrylamide gel electrophoresis. Two peaks of aspartate kinase activity could be eluted from anion exchange chromatography columns (Fast Flow Q Sepharose and Mono Q HR 5/5) with 150 and 200 mM KCl. Both peaks showed sensitivity to -lysine and the second peak in elution order was also inhibited by S-adenosylmethionine alone. Gels stained for aspartate kinase activity showed one broad band sensitive to inhibition by lysine. This band was electroeluted from the gel and further analysis showed the presence of three protein bands. The least electronegative band on the gel was identified as aspartate kinase. A third form of aspartate kinase, inhibited by threonine, was identified by gel filtration. The native Mr of the two lysine-sensitive forms of the enzyme was ca 150 000 and the threonine-sensitive enzyme 180 000, values different from those previously reported. These results confirm the hypothesis that in higher plants, at least three isoenzymic forms of aspartate kinase are present, two sensitive to lysine, the other to threonine.

AB - Aspartate kinase was purified from maize cells to near homogeneity after five steps of purification including ammonium sulphate, anion exchange chromatography, gel filtration and polyacrylamide gel electrophoresis. Two peaks of aspartate kinase activity could be eluted from anion exchange chromatography columns (Fast Flow Q Sepharose and Mono Q HR 5/5) with 150 and 200 mM KCl. Both peaks showed sensitivity to -lysine and the second peak in elution order was also inhibited by S-adenosylmethionine alone. Gels stained for aspartate kinase activity showed one broad band sensitive to inhibition by lysine. This band was electroeluted from the gel and further analysis showed the presence of three protein bands. The least electronegative band on the gel was identified as aspartate kinase. A third form of aspartate kinase, inhibited by threonine, was identified by gel filtration. The native Mr of the two lysine-sensitive forms of the enzyme was ca 150 000 and the threonine-sensitive enzyme 180 000, values different from those previously reported. These results confirm the hypothesis that in higher plants, at least three isoenzymic forms of aspartate kinase are present, two sensitive to lysine, the other to threonine.

KW - Zea mays

KW - aspartate kinase

KW - lysine

KW - threonine

KW - S-adenosyhnethionine.

U2 - 10.1016/S0031-9422(00)97516-2

DO - 10.1016/S0031-9422(00)97516-2

M3 - Journal article

VL - 31

SP - 3725

EP - 3730

JO - Phytochemistry

JF - Phytochemistry

IS - 11

ER -