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The FASEB Journal, Vol 5, 2482-2485, Copyright © 1991 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Mammalian pyruvate carboxylase: effect of biotin on the synthesis and translocation of apo-enzyme into 3T3-L adipocyte mitochondria

PM Ahmad and F Ahmad
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.

The effect of biotin on the induction (and possible requirement for uptake into mitochondria) of apopyruvate carboxylase has been examined in 3T3-L adipocytes. Cells fed biotin-sufficient medium contained only holoenzyme in mitochondria and no apoenzyme was detected. The amount of apoenzyme elaborated in biotin-deficient 3T3-L adipocytes was comparable to the holopyruvate carboxylase protein found in cells maintained on biotin-sufficient medium. Like the holoenzyme, the apoenzyme was detected exclusively in the mitochondrial fraction of 3T3- L adipocytes. This indicates that the synthesis of apopyruvate carboxylase and its translocation into mitochondria occur independently of the cofactor, biotin.


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Copyright © 1991 by The Federation of American Societies for Experimental Biology.