Purification and characterization of ribulose-1,5-bisphosphate carboxylase from triticale.

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Date
1994-04-01
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Abstract
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.
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Khan MA, Dixit A, Upadhyaya KC. Purification and characterization of ribulose-1,5-bisphosphate carboxylase from triticale. Indian Journal of Biochemistry & Biophysics. 1994 Apr; 31(2): 121-6
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https://imsear.searo.who.int/handle/123456789/27792
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Indian Journal of Biochemistry & Biophysics