Wingender-Drissen R
FEBS Lett. 1983 Oct 31;163(1):28-32. doi: 10.1016/0014-5793(83)81155-7.
We have purified cyclic AMP-dependent protein kinase from the yeast Saccharomyces cerevisiae. The purified enzyme was inactive in the absence of cyclic AMP and displayed two protein bands on SDS gel electrophoresis. One was identified as the cAMP-binding protein by chromatography on cAMP-agarose. Mr of the latter was 50 000 while the catalytic subunit had an Mr of 59 000. The enzyme accepted yeast phosphorylase, glycogen synthase and fructose 1,6-bisphosphatase as substrates. No inhibition by the mammalian protein kinase inhibitor was observed.
我们从酿酒酵母中纯化了环磷酸腺苷(cAMP)依赖性蛋白激酶。纯化后的酶在没有cAMP的情况下无活性,并且在十二烷基硫酸钠(SDS)凝胶电泳上显示出两条蛋白带。通过在cAMP-琼脂糖上进行层析,其中一条带被鉴定为cAMP结合蛋白。后者的相对分子质量(Mr)为50000,而催化亚基的Mr为59000。该酶可将酵母磷酸化酶、糖原合酶和果糖1,6-二磷酸酶作为底物。未观察到其受哺乳动物蛋白激酶抑制剂的抑制作用。