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In vivo phosphorylation of sorghum leaf phosphoenolpyruvate carboxylase
M T Guidici-Orticoni1, J Vidal, P Le Maréchal
1Laboratoire de Physiologie Végétale Moléculaire, CNRS (UA1128), Université de Paris-Sud, Orsay, France.
Biochimie
|June 1, 1988
Abstract:
The use of immunological techniques allowed us to purify close to homogeneity phosphoenolpyruvate carboxylase (PEPc, EC 4.1.1.31) from sorghum leaf. It was thus established that: 1) this protein is phosphorylated in vivo on seryl residues; 2) in C4-type photosynthesis, the phosphorylation process mainly concerns the PEPC isozyme form G; 3) enzyme phosphorylation displays significant variations through a day-night alternation which therefore suggests light control of the process.