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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Abstract 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.
AbstractList 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.
Author Akoyunoglou, G.
A. Guiali
Argyroudi-Akoyunoglou, J. H.
C. Dassiou
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Snippet The relationship between ribulose diphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase [dimerizing], EC 4.1.1.39, formerly known as carboxydismutase)...
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StartPage 443
SubjectTerms 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
Title On the Relationship between Ribulose Diphosphate Carboxylase and Protochlorophyllide Holochrome of Phaseolus vulgaris Leaves
URI https://www.jstor.org/stable/4262006
https://www.ncbi.nlm.nih.gov/pubmed/5427114
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Volume 45
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