User Settings
Article

Carboxylation of pyruvate via extramitochondrial malic enzyme in rat skeletal muscle.

Julian Świerczyński,Z. Aleksandrowicz,L Żelewski-1986-01-01-PubMed
2

TL;DRAbstract

Soluble rat skeletal muscle extract incubated in the presence of pyruvate, NaH14CO3, MgCl2 and NADP-generating system fixed H14CO3- at the rate of about 2.3 nmol/min per mg protein. The omission of pyruvate or NADPH-generating system abolished completely the fixation of H14CO3-. This suggests that malic enzyme is responsible for the carboxylation of pyruvate. A possible role of pyruvate carboxylation by extramitochondrial malic enzyme in the conversion of lactate into glycogen in skeletal muscle is discussed.

Chat with Paper

AI Agents for this Paper

Soluble rat skeletal muscle extract incubated in the presence of pyruvate, NaH14CO3, MgCl2 and NADP-generating system fixed H14CO3- at the rate of about 2.3 nmol/min per mg protein. The omission of pyruvate or NADPH-generating system abolished completely the fixation of H14CO3-. This suggests that malic enzyme is responsible for the carboxylation of pyruvate. A possible role of pyruvate carboxylation by extramitochondrial malic enzyme in the conversion of lactate into glycogen in skeletal muscle is discussed.

Keywords

Pyruvate carboxylaseCarboxylationBiochemistryMalic enzymePyruvate decarboxylationChemistryCarbon fixationPyruvate dehydrogenase complex

Chat

Click to start Chat