Jones B S, Yeaman S J, Sugden M C, Holness M J
Department of Biochemistry and Genetics, Medical School, University of Newcastle-upon-Tyne, UK.
Biochim Biophys Acta. 1992 Mar 16;1134(2):164-8. doi: 10.1016/0167-4889(92)90040-i.
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.
饥饿48小时使肝脏丙酮酸脱氢酶（PDH）激酶活性增加了74%，这是通过将[γ-32P]ATP中的32Pi掺入与E1上主要磷酸化位点对应的合成肽中直接测量得到的。给先前饥饿的大鼠随意喂食，在重新喂食后2小时内，肝脏PDH激酶活性仅被抑制了约20%，并且PDH激酶的相对高活性与PDC复合物再激活的持续抑制相关。在接下来的2小时内，PDH激酶活性没有进一步下降，而在此时间间隔内观察到PDC再激活至喂食后的水平。PDH激酶活性仅在8小时后降至喂食后的水平。
