Localization and properties of ribulose diphosphate carboxylase from castor bean endosperm
A substantial portion of the ribulose 1,5-diphosphate carboxylase activity in the endosperm of germinating castor beans (Ricinus communis var. Hale) is recovered in the proplastid fraction. The partially purified enzyme shows homology with the enzyme from spinach (Spinacia oleracea) leaves, as evidenced by its reaction against antibodies to the native spinach enzyme and to its catalytic subunit. The enzyme from the endosperm of castor beans has a molecular weight of about 500,000 and, with the exception of a higher affinity for ribulose 1,5-diphosphate, has similar kinetic properties to the spinach enzyme. The castor bean carboxylase is inhibited by oxygen and also displays ribulose 1,5-diphosphate oxygenase activity with an optimum at pH 7.5. (auth)
- Research Organization:
- Univ. of California, Santa Cruz, CA (United States)
- OSTI ID:
- 7195166
- Journal Information:
- Plant Physiol.; (United States), Vol. 55:2
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CARBOXYLASE
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
CASTOR
CATALYSIS
ENDOSPERM
ENZYMES
GERMINATION
METABOLISM
ORGANOIDS
PHOSPHATES
RIBULOSE
BIOMASS
CARBOHYDRATES
CELL CONSTITUENTS
CHEMISTRY
ENERGY SOURCES
KETONES
KINETICS
LYASES
MEDICINAL PLANTS
MONOSACCHARIDES
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PENTOSES
PHOSPHORUS COMPOUNDS
PLANT TISSUES
PLANTS
REACTION KINETICS
RENEWABLE ENERGY SOURCES
SACCHARIDES
550200* - Biochemistry