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