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Branched-chain 2-oxo acid dehydrogenase complex was resolved into component E1 and E2-kinase subcomplex by gel filtration in the presence of 1 M-NaC1. Essentially all the original activity of the complex can be regained after reconstitution of the component enzymes, reassociation being a rapid process. The specific activities of E1 and E2 were 25.1 and 19.0 units/mg respectively. Non-phosphorylated active E1 has an approx. 6-fold higher affinity for E2 than does phosphorylated E1. The components of the branched-chain 2-oxo acid dehydrogenase complex do not crossreact with the respective components from the pyruvate dehydrogenase complex. The significance of these results and of the tight association of the kinase with E2 are discussed.
K G Cook, and
A P Bradford, and
S J Yeaman
January 1988,
Methods in enzymology,
K G Cook, and
A P Bradford, and
S J Yeaman
June 1978,
FEBS letters,
K G Cook, and
A P Bradford, and
S J Yeaman
February 1986,
The Biochemical journal,
K G Cook, and
A P Bradford, and
S J Yeaman
January 1988,
Methods in enzymology,
K G Cook, and
A P Bradford, and
S J Yeaman
May 1990,
Biochimica et biophysica acta,
K G Cook, and
A P Bradford, and
S J Yeaman
January 1987,
Journal of biochemistry,
K G Cook, and
A P Bradford, and
S J Yeaman
April 1987,
Biochemical and biophysical research communications,
K G Cook, and
A P Bradford, and
S J Yeaman
May 1986,
The Biochemical journal,
K G Cook, and
A P Bradford, and
S J Yeaman
June 1983,
FEBS letters,
K G Cook, and
A P Bradford, and
S J Yeaman
April 1982,
The Biochemical journal,
