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. 1975 Feb;55(2):226–230. doi: 10.1104/pp.55.2.226

Localization and Properties of Ribulose Diphosphate Carboxylase from Castor Bean Endosperm 1

C Barry Osmond a,2, Takashi Akazawa a,3, Harry Beevers a
PMCID: PMC541589  PMID: 16659056

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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