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Plant Physiology 45:443-446 (1970)
© 1970 American Society of Plant Biologists

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Articles

On the Relationship between Ribulose Diphosphate Carboxylase and Protochlorophyllide Holochrome of Phaseolus vulgaris Leaves 1

G. Akoyunoglou, J. H. Argyroudi-Akoyunoglou, A. Guiali and C. Dassiou

a Biology Department, Nuclear Research Center "Democritus," Aghia Paraskevi Attikis, Athens, Greece

The relationship between ribulose diphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase [dimerizing], EC 4.1.1.39, formerly known as carboxydismutase) and protochlorophyllide holochrome of etiolated Phaseolus vulgaris leaves has been studied.

A procedure for partially selective extraction of the two proteins was devised using tris-HCl buffer first without and then with Triton X-100. Ribulose diphosphate carboxylase was readily extracted from etiolated bean leaves without Triton X-100, and protochlorophyllide holochrome was extracted on the addition of Triton X-100.

Optimal extraction conditions for protochlorophyllide holochrome have been found to be different for tissues of different ages.

1 Research carried out at the Nuclear Research Center "Democritus" under the auspices of the Greek Atomic Energy Commission.






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