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KMID : 0903519800230010023
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1980 Volume.23 No. 1 p.23 ~ p.30
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In Vitro Phosphorylation of Nuclear Proteins in Isolated Liver Nuclei from Rats Maintained in a Starvation State , Following Refeeding , and from Diabetic Rats with Insulin Injection
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Abstract
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Labelling of chromatin proteins with 2P was observed after incubating isolated liver nuclei with [γ-32P] ATP for 5 minutes at 37℃. The pattern of labelling with 32P was examined on SDS polyacrylamide gel electrophoresis with nuclei from rats maintained in a starvation state for 48 hours, following refeeding for 12 hours; and from fed streptozotocin-diabetic rats with insulin injection 6 hours before sacrifice.
With 48h starved rat liver nuclei the level of phosphorylation for 0.14M NaCl soluble proteins was decreased in the molecular weights between 41,000 and 200,000 dalrons relative to normal controls. Refeeding the starved rats reversed the change of phosphorylation pattern over 12 hour. The level of phosphorylation for five phenol soluble nonhistone proteins with molecular weights above 59,000 daltons was somewhat decreased with 48h starved rat liver nuclei as compared with that of normal controls. Starvation also decreased the phosphorylation level of major histones in relation to normal controls. The experiment with insulin injection into fed streptozotocin-diabetic rats show ed the tendency to increase phosphorylation of 0.14M NaCl soluble proteins (130,000 dalton protein) and phenol soluble non-histone proteins (155,000 dalton protein), The phosphorylation level of histones appeared to be invariant under the experimental conditions employed here.
These results suggest the possibility that the phosphorylation and dephosphorylation of 0.14M NaCl soluble proteins and H₁ histone precede those of other chromatin associated nuclear proteins, It is of interest to find that insulin signal was correlated to phosphorylation of nuclear proteins while glucagon signal dephosphorylated nuclear proteins.
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