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On the Relationship between Ribulose Diphosphate Carboxylase and Protochlorophyllide Holochrome of Phaseolus vulgaris Leaves
Author(s) -
G. Akoyunoglou,
J. H. ArgyroudiAkoyunoglou,
A. Guiali,
C. Dassiou
Publication year - 1970
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.45.4.443
Subject(s) - phaseolus , protochlorophyllide , pyruvate carboxylase , rubisco , chemistry , biochemistry , botany , ribulose , chlorella vulgaris , enzyme , biology , biosynthesis , algae
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.

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