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Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves.

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Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves. / Carmo-Silva, A. Elizabete; Barta, Csengele; Salvucci, Michael E.
In: Methods in Molecular Biology, Vol. 684, 24.09.2010, p. 339-347.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Carmo-Silva, AE, Barta, C & Salvucci, ME 2010, 'Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves.', Methods in Molecular Biology, vol. 684, pp. 339-347. https://doi.org/10.1007/978-1-60761-925-3_26

APA

Vancouver

Carmo-Silva AE, Barta C, Salvucci ME. Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves. Methods in Molecular Biology. 2010 Sept 24;684:339-347. doi: 10.1007/978-1-60761-925-3_26

Author

Carmo-Silva, A. Elizabete ; Barta, Csengele ; Salvucci, Michael E. / Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves. In: Methods in Molecular Biology. 2010 ; Vol. 684. pp. 339-347.

Bibtex

@article{97cb9d6c93294b5b9d94c88124a265eb,
title = "Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves.",
abstract = "Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a multifunctional enzyme that catalyzes the fixation of CO2 and O2 in photosynthesis and photorespiration, respectively. As the rate-limiting step in photosynthesis, improving the catalytic properties of Rubisco has long been viewed as a viable strategy for increasing plant productivity. Advances in biotechnology have made this goal more attainable by making it possible to modify Rubisco in planta. To properly evaluate the properties of Rubisco, it is necessary to isolate the enzyme in pure form. This chapter describes procedures for rapid and efficient purification of Rubisco from leaves of several species.",
author = "Carmo-Silva, {A. Elizabete} and Csengele Barta and Salvucci, {Michael E.}",
year = "2010",
month = sep,
day = "24",
doi = "10.1007/978-1-60761-925-3_26",
language = "English",
volume = "684",
pages = "339--347",
journal = "Methods in Molecular Biology",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves.

AU - Carmo-Silva, A. Elizabete

AU - Barta, Csengele

AU - Salvucci, Michael E.

PY - 2010/9/24

Y1 - 2010/9/24

N2 - Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a multifunctional enzyme that catalyzes the fixation of CO2 and O2 in photosynthesis and photorespiration, respectively. As the rate-limiting step in photosynthesis, improving the catalytic properties of Rubisco has long been viewed as a viable strategy for increasing plant productivity. Advances in biotechnology have made this goal more attainable by making it possible to modify Rubisco in planta. To properly evaluate the properties of Rubisco, it is necessary to isolate the enzyme in pure form. This chapter describes procedures for rapid and efficient purification of Rubisco from leaves of several species.

AB - Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a multifunctional enzyme that catalyzes the fixation of CO2 and O2 in photosynthesis and photorespiration, respectively. As the rate-limiting step in photosynthesis, improving the catalytic properties of Rubisco has long been viewed as a viable strategy for increasing plant productivity. Advances in biotechnology have made this goal more attainable by making it possible to modify Rubisco in planta. To properly evaluate the properties of Rubisco, it is necessary to isolate the enzyme in pure form. This chapter describes procedures for rapid and efficient purification of Rubisco from leaves of several species.

U2 - 10.1007/978-1-60761-925-3_26

DO - 10.1007/978-1-60761-925-3_26

M3 - Journal article

C2 - 20960141

AN - SCOPUS:79952117686

VL - 684

SP - 339

EP - 347

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -