Issue Archive

The effects of extracellular calmodulin on protein phosphorylation in cytoplasmic fraction from suspension-cultured tobacco (Nicotiana tobacum L.) cells

Zhang Laiqun, Li Fang, Sun Daye

Institute of Molecular Biology,Hebei Normal University.Shijiazhuang 050016,Hebei

Abstract

The effects of extracellular calmodulin on the activity of protein phosphorylation were studied in suspension-cultured tobacco cells. The activity of protein phosphorylation in cytoplasmic fraction increased gradually as measured in different culture days, as it reaches peak then decrease. On its peak day, the activityof protein phosphorylation could be blocked by the anti-CaM serum, and addition of exogenous purified CaM could eliminate the inhibitory effects of anti-CaM serum. The activity of protein phosphorylation of cytoplasmic fraction from suspension-cultured tobacco cells was also activated by pure CaM. The activation was time- and dose-dependent. The extracellular CaM induced activation of protein phosphorylatino was different from red light induced one with respect to their time courses.

Key words: Suspension cultured tobacco cells;Extracellular CaM;Protein phosphorylation

Received: 　　Accepted:

Corresponding author: 　　E-mail:

Citing This Article：

Zhang Laiqun, Li Fang, Sun Daye. The effects of extracellular calmodulin on protein phosphorylation in cytoplasmic fraction from suspension-cultured tobacco (Nicotiana tobacum L.) cells. Acta Physiol Sin 2001; 53 (3): (in Chinese with English abstract).