Panin L E, Tret'iakova T A
Biull Eksp Biol Med. 1981 Aug;92(8):37-9.
The rates of glycolysis and glycogenolysis an the rate of lactate formation from glucoso-6-phosphate (G-6-Ph) in the liver were reduced during stress (starvation). On the contrary, these activities in the adrenals were increased. The rates of lactate formation from fructose diphosphate remained unchanged in both organs. The results obtained attest to the inhibition in the liver and activation in the adrenals of phosphorylase, hexokinase and phosphofructokinase. The degree of hexokinase inhibition in the liver depended on the presence of cAMP, ATP and MgCl2 in the incubation medium and was a consequence of enzymatic phosphorylation. Unlike 2', 3'-AMP, the inhibitory effect of CAMP was highly specific. The protein inhibitor of protein kinase completely reversed the inhibitory effect of cAMP on hexokinase. In the adrenals, cAMP slightly increased the rates of glycolysis and lactate formation from G-6-Ph because of allosteric effects of cAMP. The activation rather than inhibition of glycolysis in the adrenals during stress is probably caused by the absence in this tissue of cAMP-dependent protein kinase which phosphorylates hexokinase.
在应激（饥饿）期间，肝脏中糖酵解和糖原分解的速率以及由6-磷酸葡萄糖（G-6-Ph）生成乳酸的速率均降低。相反，肾上腺中的这些活性增加。两个器官中由二磷酸果糖生成乳酸的速率均保持不变。所得结果证明肝脏中磷酸化酶、己糖激酶和磷酸果糖激酶受到抑制，而肾上腺中这些酶被激活。肝脏中己糖激酶的抑制程度取决于孵育介质中cAMP、ATP和MgCl2的存在，并且是酶促磷酸化的结果。与2',3'-AMP不同，cAMP的抑制作用具有高度特异性。蛋白激酶的蛋白抑制剂完全逆转了cAMP对己糖激酶的抑制作用。在肾上腺中，由于cAMP的变构效应，cAMP略微增加了糖酵解速率以及由G-6-Ph生成乳酸的速率。应激期间肾上腺中糖酵解的激活而非抑制可能是由于该组织中不存在使己糖激酶磷酸化的cAMP依赖性蛋白激酶所致。
