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  • Title: Spermine specifically inhibits the phosphorylation of an 11,000-dalton nuclear protein in various cultured mammalian cell lines.
    Author: Chen KY, Verma R.
    Journal: Biochem Biophys Res Commun; 1984 Feb 14; 118(3):710-6. PubMed ID: 6704103.
    Abstract:
    The effect of polyamines (putrescine, spermidine and spermine) on endogenous protein phosphorylation in mouse neuroblastoma cells was investigated by using techniques of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The results indicated that spermine at 1mM completely inhibited the phosphorylation of the 11,000-dalton and 120,000-dalton proteins in nuclear fractions. The inhibition of the phosphorylation of the 11,000-dalton but not the 120,000-dalton protein by spermine was also observed in five other cell lines examined and appeared to be a general phenomenon. The inhibitory effect of spermine on the phosphorylation of the 11,000-dalton protein was specific, other cations such as ammonium chloride, arginine, putrescine, cyclen and trien were ineffective at equal molar or much higher concentrations.
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