Purification and characterization of ribulose-1,5-bisphosphate carboxylase from triticale.
Indian J Biochem Biophys
;
1994 Apr; 31(2): 121-6
Artigo
em Inglês
| IMSEAR
| ID: sea-27792
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.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Ribulose-Bifosfato Carboxilase
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Sais
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Cinética
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Cátions
/
Grão Comestível
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Cromatografia em Gel
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Eletroforese em Gel de Poliacrilamida
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Ativação Enzimática
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Peso Molecular
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1994
Tipo de documento:
Artigo
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