-transparent.png){kind=logo}
Starvation for 48 h elicited a 74% increase in hepatic pyruvate dehydrogenase (PDH) kinase activity, measured directly by 32Pi-incorporation from [gamma-32P]ATP into a synthetic peptide corresponding to the major phosphorylation site on E1. The administration of chow ad libitum to previously-starved rats suppressed hepatic PDH kinase activity by only approx. 20% within 2 h of re-feeding, and the relatively high activity of PDH kinase was associated with continued suppression of PDC complex re-activation. Whereas there was no further decline in PDH kinase activity over the next 2 h, PDC re-activation to the fed value was observed during this time interval. PDH kinase activity decreased to fed values only after 8 h.
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
August 1990,
Biochemical Society transactions,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
March 1989,
The Biochemical journal,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
January 1989,
Annals of the New York Academy of Sciences,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
May 1990,
The Biochemical journal,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
October 1990,
Biochemical Society transactions,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
October 1990,
Biochemical Society transactions,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
October 1989,
The Biochemical journal,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
October 1997,
Biochimica et biophysica acta,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
November 1993,
The Biochemical journal,
B S Jones, and
S J Yeaman, and
M C Sugden, and
M J Holness
September 1996,
Molecular and cellular biochemistry,
