Isoenzyme of Pyruvate Kinase in Proplastids from Developing Castor Bean Endosperm | Zendy

Vincenzo De Luca | Zendy; David T. Dennis | Zendy

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Isoenzyme of Pyruvate Kinase in Proplastids from Developing Castor Bean Endosperm

Author(s) -

Vincenzo De Luca,

David T. Dennis

Publication year - 1978

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.61.6.1037

Subject(s) - endosperm , pyruvate kinase , ricinus , biochemistry , sephadex , biology , isozyme , organelle , enzyme , glycolysis

Proplastids from developing castor bean (Ricinus communis) endosperm have a pyruvate kinase activity which is extremely unstable on isolation from the organelle. It can be stabilized by 20 mm 2-mercaptoethanol in 20% ethylene glycol. In contrast the soluble pyruvate kinase is stable at 60 C for 10 minutes. The two activities have different pH optima. The soluble and the proplastid activities are eluted from a diethylaminoethyl-Sephadex A-25 sievorptive column at different ionic strengths.

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