| Autor: |
Zbigniew Kaniuga, Joanna Kwast-Welfeld |
| Rok vydání: |
1981 |
| Předmět: |
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| Zdroj: |
The International journal of biochemistry. 13(6) |
| ISSN: |
0020-711X |
| Popis: |
1. 1. Two isozymes of cAMP-dependent protein kinases which can be separated by DEAE-cellulose chromatography, have been found in both the supernatant and the paniculate fraction of chick liver obtained following the centrifugation of homogenate at 27,000 g. 2. 2. Fraction I was abundant in the supernatant while Fraction II was bound to the particulate subfraction of liver cells at all stages of developing chick as well as in the soluble subfraction of liver cells of the embryo and the newly hatched chick. 3. 3. The particulate-bound enzyme could be solubilized in the presence of Triton X-100 during homogenization. 4. 4. Both isozymes of protein kinases exhibited the maximum activity at the mild embryogenesis and declined at the time of hatching in both the supernatant and the particulate subfractions of liver cells. In contrast to the activity of Fraction II which increased in the particulate subfraction of liver cells during the postnatal development of chick and the activity of Fraction I was enhanced only in the supernatant. 5. 5. An elevation of cAMP level in the homogenate of chick liver resulted in a decrease of cAMP-dependent protein kinase Fraction II activity and an increase of that in the particulate subfraction. These observations suggest a translocation of holoenzyme of cAMP-dependent protein kinase Fraction II from the cytosol to the particulate subfraction. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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