Studies on the mechanism of activation of mitotic histone H1 kinase.
Studies on the mechanism of activation of mitotic histone H1 kinase.
复制标题
有丝分裂组蛋白H1激酶激活机制的研究。
DOI：
10.1016/0006-291x(80)91625-3
复制
发表时间：
1980
影响因子：
3.1
通讯作者：
Langan,TA
中科院分区：
文献类型：
--
作者：
Zeilig,CE;Langan,TA
在同步化的Novikoff肝癌细胞中检测到染色质相关的组蛋白H1激酶。酶比活性增加4至6倍，从晚G-2中期中期，然后呈指数衰减（T1 2，28.5分钟）的间期水平。有丝分裂激酶的提取物保留在37° C下体外衰变的能力，但在0° C下（T 12，24 min），在其中间期活性稳定的条件下。在蔗糖密度梯度的间期和有丝分裂酶（衰减前后）的沉降率是相同的。纯化并不改变酶的衰减速率。然而，高离子强度防止有丝分裂酶的粗品而非纯化制剂的衰变。结果进行了讨论的变构机制的可逆激活酶的活性。
A chromatin-associated histone H1 kinase has been detected in synchronized Novikoff hepatoma cells. Enzyme specific activity increased 4 to 6-fold from late G-2 to mid-metaphase, then decayed exponentially (T 1 2, 28.5 min) to the interphase level. Extracts of the mitotic kinase retained the ability to decay in vitro at 37° C but not at 0° C (T 1 2, 24 min), under conditions in which interphase activity was stable. Sedimentation rates in sucrose density gradients of interphase and mitotic enzymes (before and after decay) were identical. Purification did not alter the rate of enzyme decay. However, high ionic strength prevented decay of crude but not purified preparations of mitotic enzyme. The results are discussed in terms of an allosteric mechanism for reversible activation of enzyme activity.