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Studies on the kinetics of cation-associated fluorescence changes in chloroplast membranes
Authors:RC Jennings  PD Gerola  FM Garlaschi  G Forti
Institution:Centro di Studio del CNR per la Biologia Cellulare e Molecolare delle Piante, Istituto di Scienze Botaniche dell''Università degli Studi, Via Giuseppe Colombo, 60, 20133 Milano, Italy
Abstract:A soluble Ca2+- and Ca2+—calmodulin-activated protein kinase was partially purified from wheat germ. The phosphorylation of histones and casein catalyzed by this enzyme is largely Ca2+-dependent. After repeated gel filtration of the protein kinase in the presence of 1 mM EGTA, the phosphorylation of casein and histones by the enzyme is activated 3-fold and up to 16-fold, respectively, by added calmodulin (12.5 μM). Such activation of the protein kinase by calmodulin is Ca2+-dependent. The protein kinase binds to calmodulin—Sepharose 4B in a Ca2+-dependent fashion. This type of Ca2+-activated protein kinase may be involved in stimulus—response coupling in plants.
Keywords:DCMU  3-(3  4 dichlorophenyl)-1  1 dimethylurea  LHCP  light harvesting chlorophyll-protein complex  PS  photosystem
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