Biomedical subjects

J Palvimo

Publications and source records attributed to J Palvimo.

21 records · Page 2Linked to original sources

PubMed1985

Thiophosphorylation and phosphorylation of chromatin proteins from calf thymus in vitro.

Thiophosphorylation and phosphorylation of 5% perchloric acid extractable proteins from calf thymus chromatin were studied using a cyclic GMP-dependent protein kinase from bovine lung and a nuclear protein kinase II from rat liver. The phosphorylation reaction catalyzed by nuclear protein kinase II utilized [gamma -35S]ATP as a phosphate donor almost as efficiently as [gamma -32P]ATP, but the cGMP-dependent protein kinase mediated phosphorylation by [35S]ATP was about 20 times less effective than that by [32P]ATP. In addition, using [35S]ATP instead of [32P]ATP changed markedly the cGMP-dependent phosphorylation pattern of the PCA-extractable proteins as examined by gel electrophoresis. Thus, depending on the type of protein kinase, the results from thiophosphorylation and phosphorylation reactions may vary considerably.

Amino Acids↗

PubMed1984

Polyamines and heparin do not appreciably influence phosphorylation of chromatin proteins HMG 14 and HMG 17 by nuclear protein kinase II.

Phosphorylation of acidic substrates such as casein and phosvitin by nuclear protein kinase II is stimulated by polyamines and inhibited by heparin, which mimics an endogenous proteoglycan inhibitor. The phosphorylation in vitro of the chromatin proteins HMG 14 and HMG 17 by nuclear protein kinase II were examined in this study focusing on the modifying effects of polyamines and heparin. Both HMG proteins were phosphorylated by the enzyme, but polyamines did not appreciably influence the extent of their phosphorylation. In addition, heparin did not inhibit the kinase reaction with the HMG proteins as substrates. These results indicate that the nuclear protein kinase II does actively phosphorylate HMG 14 and HMG 17 in vitro but that in contrast to some model substrates, polyamines and heparin do not appreciably affect their phosphorylation.

Animals↗

PubMed1983

Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase.

Phosphorylation of HMG 14 proteins from calf thymus and avian erythrocytes was studied using a cyclic GMP-dependent protein kinase from bovine lung. HMG 14 from calf thymus was a good substrate for the enzyme, but HMG 14 from avian erythrocytes was not phosphorylated. Of the potential phosphorylation sites, the one in the amino terminal sequence Pro-Lys-Arg-Lys-Val-Ser-Ser-Ala-Glu (residues 1-9) is present in HMG 14 from calf thymus but not in HMG 14 from avian erythrocytes suggesting that the phosphorylated amino acid residue in HMG 14 from calf thymus is Ser-6 (and possibly Ser-7).

Animals↗