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

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...

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Published inPlant physiology (Bethesda) Vol. 45; no. 4; pp. 443 - 446
Main Authors Akoyunoglou, G., Argyroudi-Akoyunoglou, J. H., A. Guiali, C. Dassiou
Format Journal Article
LanguageEnglish
Published United States American Society of Plant Physiologists 01.04.1970
Subjects
Carboxy-Lyases - metabolism
Chloroplasts
Chromium
Diphosphates
Enzymes
Leaves
Nuclear research
Pentosephosphates
Phosphates
Plant Proteins - isolation & purification
Plants
Plants, Edible - metabolism
Spinach
Surface-Active Agents
Ultrafiltration
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0032-0889
1532-2548
DOI:10.1104/pp.45.4.443