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Mammalian pyruvate carboxylase: effect of biotin on the synthesis and translocation of apo‐enzyme into 3T3‐L adipocyte mitochondria
Author(s) -
Ahmad Patricia M.,
Ahmad Fazal
Publication year - 1991
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.5.10.2065895
Subject(s) - pyruvate carboxylase , biotin , acetyl coa carboxylase , biochemistry , mitochondrion , enzyme , cofactor , adipocyte , chromosomal translocation , chemistry , biology , adipose tissue , gene
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 mitochrondria 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.—Ahmad, P. M.; Ahmad, F. Mammalian pyruvate carboxylase. FASEB J. 5: 2482–2485; 1991.