| Autor: |
Pete John, Donato Chiatante, Paola Brusa, Mariacristina Crosti, Anthony J. Trewavas |
| Rok vydání: |
1993 |
| Předmět: |
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| Zdroj: |
Plant Science. 89:13-21 |
| ISSN: |
0168-9452 |
| Popis: |
Protein kinase activity was detected in a 0.5-M NaCl soluble protein extract obtained from nuclei purified after 24 h of germination from pea root meristematic tissue. Permeation chromatography of this extract resolved several different protein kinase activities. One was Ca2+-dependent and was able to phosphorylate histone and casein as exogenous substrates to the incubation mixture. Another one was stimulated by the presence of Mg2+ under Ca2+-free condition. Two proteins (of 33.1 and 34.6 kDa) present in this extract were specifically recognised by the EGV antibody (an antibody raised against a conserved region of the p34cdc2protein kinase). It is proposed that part of the Ca2+-independent protien kinase activity solubilised from plant nuclei is contributed by a p34cdc2-like protein kinase and the possible functions of nuclear p34cdc2-like proteins during germination are discussed. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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