By Gerald Litwack (Eds.)
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Additional info for Biochemical Actions of Hormones. Volume 6
2. During the extraction procedure no dissociation of the subunits oc curs. 3. The assay conditions are established such that the measured activity or activity ratio does not reflect the concentration of endogenous components of the extraction media other than the protein kinase. In general, the techniques that are required to meet the first criterion have received the greatest attention. This is a pragmatic approach, but as such it should be appreciated that an understanding of the action of the hormone can be inferred only on the assumption that dissociation of the protein kinase is essential for activation.
This group has also reported that levels of catalytic subunit in the nucleus are enhanced during the process of liver regeneration, presumably as a conse quence of elevated cAMP. It is apparent that studies of potential translocation of protein kinase subunits are not easy and that measurement of activities in cellular fractions may well be compromised by the difficulty of determining the extent of nonspecific association. The results of this type of study are presented below, but must be interpreted within the reservations expressed above.
Cytoplasmic and nuclear protein kinase activity in control and Bt2-cAMP-stimulated perfused rat liver. Livers were removed 8 minutes after addition of either water or of 100 μ Μ Bt2-cAMP addition to the perfusate. 5μ Μ cAMP, respectively. Protein kinase activity was corrected for incorporation in the absence of exogenous substrate. Data are presented on the basis of nmoles 3 2 P0 4 incorporated per minute into histone either per mg of cytoplasmic or nuclear protein (top) or per gm of liver (bottom).
Biochemical Actions of Hormones. Volume 6 by Gerald Litwack (Eds.)