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 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.
D002262:Carboxy-Lyases / Q000378:metabolism*; D010428:Pentosephosphates; D010940:Plant Proteins / Q000302:isolation & purification*; D010945:Plants, Edible / Q000378:metabolism*; D013501:Surface-Active Agents
D010428:Pentosephosphates; D010940:Plant Proteins; D013501:Surface-Active Agents; D002262:Carboxy-Lyases