小麦胚乳依赖钙的蛋白激酶与钙调蛋白拮抗剂和多胺的相互作用。
Interaction of wheat germ ca-dependent protein kinases with calmodulin antagonists and polyamines.
机构信息
Department of Biochemistry, La Trobe University, Bundoora, Victoria, 3083, Australia.
出版信息
Plant Physiol. 1985 Dec;79(4):968-72. doi: 10.1104/pp.79.4.968.
The two soluble Ca(2+)-dependent protein kinases resolved from wheat (Triticum aestivum) embryo (protein kinases I and II) are inhibited by the phenothiazine-derived calmodulin antagonists trifluoperazine fluphenazine, and chlorpromazine. Protein kinases I and II are also inhibited by a variety of other calmodulin antagonists (including calmidazolium, amitriptyline, and iprindole), phosphodiesterase inhibitors (including flufenamic acid and papavarine) and by lanthanides. A number of compounds that inhibit mammalian Ca(2+) - and phospholipid-activated protein kinase (protein kinase C) including quercetin, polymixin B sulfate, and polyamines (as well as phenothiazine derivatives) also inhibit protein kinases I and II. Poly-l-lysine and poly-l-ornithine activate both plant Ca(2+)-dependent protein kinases.
从小麦（Triticum aestivum）胚中分离得到的两种可溶性 Ca(2+)-依赖性蛋白激酶（蛋白激酶 I 和 II）被苯并噻嗪衍生的钙调蛋白拮抗剂三氟拉嗪、氟奋乃静和氯丙嗪抑制。蛋白激酶 I 和 II 也被多种其他钙调蛋白拮抗剂（包括 calmidazolium、阿米替林和 iprindole）、磷酸二酯酶抑制剂（包括 flufenamic acid 和罂粟碱）和镧系元素抑制。许多抑制哺乳动物 Ca(2+) 和磷脂激活蛋白激酶（蛋白激酶 C）的化合物，包括槲皮素、多粘菌素 B 硫酸盐和多胺（以及苯并噻嗪衍生物），也抑制蛋白激酶 I 和 II。聚赖氨酸和聚鸟氨酸激活植物 Ca(2+)-依赖性蛋白激酶。
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