cAMP-dependent protein kinase II interactions with nuclei derived from rat mammary tumor.

F Y Tang, L S Catapano
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Abstract

cAMP-dependent protein kinase from bovine heart exhibited significant interactions with nuclei from rat mammary tumors. These enzyme-nuclear interactions occurred when the intact holoenzyme was preincubated with 10 nM cAMP, 1 mM MgATP at 24 degrees C to produce high-affinity monophasic cAMP-dissociation kinetics. The enzyme-nuclear interactions are correlated with the loss of cAMP and PO4 from the purified enzyme. The data indicate that the high affinity cAMP-dependent protein kinase II exhibits significant nuclear interaction which may be related to cAMP function in rat mammary tumors.

camp依赖性蛋白激酶II与大鼠乳腺肿瘤细胞核的相互作用。
牛心脏camp依赖性蛋白激酶与大鼠乳腺肿瘤细胞核表现出显著的相互作用。当完整的全酶与10 nM cAMP, 1 mM MgATP在24℃下预孵育时,这些酶核相互作用发生,产生高亲和力的单相cAMP解离动力学。酶核相互作用与纯化酶中cAMP和PO4的损失有关。这些数据表明,高亲和力的cAMP依赖性蛋白激酶II在大鼠乳腺肿瘤中表现出显著的核相互作用,这可能与cAMP功能有关。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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