Purification and characterization of ribulose-1,5-bisphosphate carboxylase from triticale.
Ribulose-1,5-bisphosphate carboxylase has been isolated from a synthetic cereal triticale and purified using a newly developed rapid procedure involving precipitation with ammonium sulphate (35-55% saturation), DEAE-cellulose (DE-52) chromatography and filtration through Sepharose CL-68. Molecular weights of the enzyme subunits are 15.5 and 52 kDa which corresponds to 540 kDa for the hexadecameric holoenzyme. Isoelectric focussing showed that the enzyme has a pI of 4.2. Various kinetic constants determined under aerobic conditions are: Km (CO2), 118 microM; Km (RuBP), 220 microM (at 20 mM NaHCO3) and Vmax, 690 nmole CO2 fixed/mg enzyme/min.
Khan
M A
MA
School of Life Sciences, Jawaharlal Nehru University, New Delhi.
Dixit
A
A
Upadhyaya
K C
KC
D002412:Cations; D002850:Chromatography, Gel; D002523:Edible Grain / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007700:Kinetics; D008970:Molecular Weight; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D012492:Salts / Q000494:pharmacology
D002412:Cations; D012492:Salts; D012273:Ribulose-Bisphosphate Carboxylase