PMID: 41585Oct 26, 1979

Immunochemical aspects, molecular and kinetic properties of multiple forms of acetyl-CoA acetyltransferase from rat liver mitochondria

Biochimica Et Biophysica Acta
D Schwabe, W Huth

Abstract

Acetyl-CoA acetyltransferase (EC 2.3.1.9) from rat liver mitochondria, which catalyzes the first step in the biosynthesis of ketone bodies, exists in two forms, designated transferase A and transferase B. Both transferases showed immunochemical cross-reactivity, but are immunologically unrelated to cytosolic acetyl-CoA acetyltransferase activity and the mitochondrial acetyl-CoA acyltransferase from rat liver. The transferases A and B were estimated to have molecular weights of 151 000 in the absence and 40 000 in the presence of sodium dodecyl sulfate. They differ with respect to charge states and multiplicity of forms as indicated by isoelectric focusing. Transferase A appeared in two forms with isoelectric points of 8.4 and 9.1, whereas transferase B represents a stable protein state with an isoelectric point of 9.0. Kinetic analysis of the reactions leading to acetoacetyl-CoA synthesis revealed saturation curves with multiple intermediary plateaus, indicating a complex kinetic behaviour. The data presented are interpreted as representing a microheterogeneity of forms of the mitochondrial acetyl-CoA acetyltransferase. The kinetic properties exhibited suggest a role for this microheterogeneity in the regulation of ketogenesis.

Citations

Aug 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·M G Hartmanis, T C Stadtman
Mar 15, 1988·European Journal of Biochemistry·W HuthU Möller

Related Concepts

Acetyl-CoA C-Acetyltransferase
Acetyl-CoA C-Acyltransferase
Acetyltransferase
Acyltransferase
Metazoa
Cross Reactions
Cytoplasmic Matrix
Immunodiffusion Measurement
Mitochondria, Liver
Rats, Laboratory

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