Synthesis of two non-phosphorylated proteins induced in mouse L-cells by homologous interferon |
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Authors: | Alain Pauloin Marie-Françoise Dubois |
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Institution: | INSERM U-43 Hopital Saint Vincent de Paul 74, avenue Denfert Rochereau 75014 Paris, France |
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Abstract: | We have shown that two proteins P1 and P2 of Mr 43000 and 40800 are always detected by two-dimensional gel electrophoresis of interferon-treated mouse L-929 cell extract. These two proteins have an isoelectric point of pH 4.6 and pH 4.7 respectively. If Pl is detectable in small amount in the control gels, P2 is completely absent. Actinomycin D added at the same time as interferon, prevents both P1 and P2 synthesis, but enhances their production when added between 4 to 6 h after interferon. Using molecular weight and isoelectric point as criteria, we have tried to compare P1 and P2 to enzymes induced by interferon. With double-labelled two-dimensional gels by |35S| methionine and |γ32P| ATP, we have shown that neither P1 nor P2 is phosphorylated. This experimental procedure has allowed us to obtain new data on substrates phosphorylared by interferon induced protein kinase. |
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Keywords: | double-stranded RNA dsRNA Nonidet P40 NP40 poly(riboinosinic) poly(ribocytidilic)acid poly(I)poly(C) sodium dodecyl sulfate SDS two dimensional gel 2-D gel |
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