Phosphorylation in vivo of non-ribosomal proteins from native 40 S ribosomal particles of Krebs II mouse ascites-tumour cells
Keyword(s):
Four non-ribosomal proteins from native 40 S ribosomal subunits with mol.wts. of 110 000, 84 000, 68 000 and 26 000 were phosphorylated in vivo when ascites cells were incubated in the presence of [32P]Pi. The 110 000-, 84 000- and 26 000-dalton proteins are identical with phosphorylated products from native 40 S subunits after phosphorylation in vitro by a cyclic nucleotide-independent protein kinase. Phosphoserine was the major phosphorylated amino acid of the proteins phosphorylated in vivo and in vitro.
1979 ◽
Vol 88
(4)
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pp. 1275-1283
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1991 ◽
Vol 11
(6)
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pp. 3027-3036
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1991 ◽
Vol 11
(6)
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pp. 3027-3036
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1990 ◽
Vol 10
(6)
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pp. 2820-2831
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2006 ◽
Vol 27
(5)
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pp. 1581-1591
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