|
KMID : 0578319940040020159
|
|
Molecules and Cells
1994 Volume.4 No. 2 p.159 ~ p.166
|
|
|
A Calcium-Dependent Protein Kinase Regulated by Phytochrome Action in Oats
|
|
Kim, Tae In
Cho, Tae Ju/Chae, Quae
|
|
|
Abstract
|
|
|
|
A calcium-dependent protein kinase (79 kDa) regulated by phytochrome action was partially purified from the cytosolic fraction of oat tissue. The enzyme was significantly activated by phosphatidylserine (PtdSer) at Cat+ concentrations of 10-6-10-5 M. One characteristic observed was that this enzyme was activated by an unsaturated fatty acid, linoleic acid in the absence of Ca", but inhibited at 10-5-10-4 M concentration range of Caz+. In contrast, the enzyme activity was not changed by the saturated fatty acid, arachidic acid. This protein kinase was purified 1,000-fold by poly-lysine agarose column chromatography, after which the it had a specific activity of 21 nmole/min/mg, and two protein bands (79 kDa, 48 kDa) were observed after separation by SDS-PAGE and silver staining. Among these two proteins, the 79 kDa protein was identified as a protein kinase by its phosphorylation in a highly purified fraction in the absence of exogenous substrate. In an in vitro assay system, a drastic enhancement of the enzyme activity was observed in response to irradiation with red fight ´t not with far-red light in comparison to controls that were not irradiated.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|