Home > Research > Publications & Outputs > Regulation of Lysine Metabolism and Endosperm P...

Research

Links

Text available via DOI:

Keywords

View graph of relations

Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations. / Azevedo, Ricardo A.; Lea, Peter John; Damerval, Catherine et al.
In: Journal of Agricultural and Food Chemistry, Vol. 52, No. 15, 2004, p. 4865-4871.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Azevedo, RA, Lea, PJ, Damerval, C, Landry, J, Bellato, CM, Meinhardt, LW, Le Guilloux, M, Delhaye, S, Varisi, VA, Gaziola, SA, Gratão, PL & Toro, AA 2004, 'Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations.', Journal of Agricultural and Food Chemistry, vol. 52, no. 15, pp. 4865-4871. https://doi.org/10.1021/jf035422h

APA

Azevedo, R. A., Lea, P. J., Damerval, C., Landry, J., Bellato, C. M., Meinhardt, L. W., Le Guilloux, M., Delhaye, S., Varisi, V. A., Gaziola, S. A., Gratão, P. L., & Toro, A. A. (2004). Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations. Journal of Agricultural and Food Chemistry, 52(15), 4865-4871. https://doi.org/10.1021/jf035422h

Vancouver

Azevedo RA, Lea PJ, Damerval C, Landry J, Bellato CM, Meinhardt LW et al. Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations. Journal of Agricultural and Food Chemistry. 2004;52(15):4865-4871. doi: 10.1021/jf035422h

Author

Azevedo, Ricardo A. ; Lea, Peter John ; Damerval, Catherine et al. / Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations. In: Journal of Agricultural and Food Chemistry. 2004 ; Vol. 52, No. 15. pp. 4865-4871.

Bibtex

@article{d87c90bec81a4f3ea24d5472f513c35b,
title = "Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations.",
abstract = "Two high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine, were reduced in relation to the wild-type lines B77xB79+ and B37+. These alterations in the storage protein fraction distribution possibly explain the increased concentration of lysine in the two mutants. Using two-dimensional polyacrylamide gel electrophoresis of proteins of mature grains, variable amounts of zein polypeptides were detected and considerable differences were noted between the four lines studied. The analysis of the enzymes involved in lysine metabolism indicated that both mutants have reduced lysine catabolism when compared to their respective wild types, thus allowing more lysine to be available for storage protein synthesis.",
keywords = "Aspartate kinase, lysine, lysine 2-oxoglutarate reductase, maize, storage proteins",
author = "Azevedo, {Ricardo A.} and Lea, {Peter John} and Catherine Damerval and Jacques Landry and Bellato, {Cl{\'a}udia M.} and Meinhardt, {Lyndel W.} and {Le Guilloux}, Martine and Sonia Delhaye and Varisi, {Vanderlei A} and Gaziola, {Salete A.} and Grat{\~a}o, {Priscila Lupino} and Toro, {Alejandro A.}",
year = "2004",
doi = "10.1021/jf035422h",
language = "English",
volume = "52",
pages = "4865--4871",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "15",

}

RIS

TY - JOUR

T1 - Regulation of Lysine Metabolism and Endosperm Protein Synthesis by the Opaque-5 and Opaque-7 Maize Mutations.

AU - Azevedo, Ricardo A.

AU - Lea, Peter John

AU - Damerval, Catherine

AU - Landry, Jacques

AU - Bellato, Cláudia M.

AU - Meinhardt, Lyndel W.

AU - Le Guilloux, Martine

AU - Delhaye, Sonia

AU - Varisi, Vanderlei A

AU - Gaziola, Salete A.

AU - Gratão, Priscila Lupino

AU - Toro, Alejandro A.

PY - 2004

Y1 - 2004

N2 - Two high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine, were reduced in relation to the wild-type lines B77xB79+ and B37+. These alterations in the storage protein fraction distribution possibly explain the increased concentration of lysine in the two mutants. Using two-dimensional polyacrylamide gel electrophoresis of proteins of mature grains, variable amounts of zein polypeptides were detected and considerable differences were noted between the four lines studied. The analysis of the enzymes involved in lysine metabolism indicated that both mutants have reduced lysine catabolism when compared to their respective wild types, thus allowing more lysine to be available for storage protein synthesis.

AB - Two high lysine maize endosperm mutations, opaque-5 (o5) and opaque-7 (o7), were biochemically characterized for endosperm protein synthesis and lysine metabolism in immature seeds. Albumins, globulins, and glutelins, which have a high content of lysine, were shown to be increased in the mutants, whereas zeins, which contain trace concentrations of lysine, were reduced in relation to the wild-type lines B77xB79+ and B37+. These alterations in the storage protein fraction distribution possibly explain the increased concentration of lysine in the two mutants. Using two-dimensional polyacrylamide gel electrophoresis of proteins of mature grains, variable amounts of zein polypeptides were detected and considerable differences were noted between the four lines studied. The analysis of the enzymes involved in lysine metabolism indicated that both mutants have reduced lysine catabolism when compared to their respective wild types, thus allowing more lysine to be available for storage protein synthesis.

KW - Aspartate kinase

KW - lysine

KW - lysine 2-oxoglutarate reductase

KW - maize

KW - storage proteins

U2 - 10.1021/jf035422h

DO - 10.1021/jf035422h

M3 - Journal article

VL - 52

SP - 4865

EP - 4871

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 15

ER -