Localization and properties of ribulose diphosphate carboxylase from castor bean endosperm

Journal Article · Fri Jan 31 23:00:00 EST 1975 · Plant Physiol.; (United States)

DOI:https://doi.org/10.1104/pp.55.2.226· OSTI ID:7195166

Osmond, C B; Akazawa, T; Beevers, H

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
• OSTI ID: 7195166
• Journal Information: Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 55:2; ISSN PLPHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
BIOMASS
CARBOHYDRATES
CARBOXYLASE
CASTOR
CATALYSIS
CELL CONSTITUENTS
CHEMISTRY
ENDOSPERM
ENERGY SOURCES
ENZYMES
GERMINATION
KETONES
KINETICS
LYASES
MEDICINAL PLANTS
METABOLISM
MONOSACCHARIDES
ORGANIC COMPOUNDS
ORGANOIDS
OXYGEN COMPOUNDS
PENTOSES
PHOSPHATES
PHOSPHORUS COMPOUNDS
PLANT TISSUES
PLANTS
REACTION KINETICS
RENEWABLE ENERGY SOURCES
RIBULOSE
SACCHARIDES