> top > projects > sentences > docs > PubMed:8288564 > annotations

PubMed:8288564 JSONTXT 20 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1 0-74 Sentence denotes Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1.
T1 0-74 Sentence denotes Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1.
T2 75-164 Sentence denotes Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase.
T2 75-164 Sentence denotes Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase.
T3 165-329 Sentence denotes We have previously reported the existence of two different molecular species of protein methylase I (S-adenosylmethionine:protein-arginine N-methyltransferase, E.C.
T3 165-329 Sentence denotes We have previously reported the existence of two different molecular species of protein methylase I (S-adenosylmethionine:protein-arginine N-methyltransferase, E.C.
T4 330-429 Sentence denotes 2.1.1.23) in calf brain, one specific for myelin basic protein and the other for histone (Ghosh, S.
T4 330-429 Sentence denotes 2.1.1.23) in calf brain, one specific for myelin basic protein and the other for histone (Ghosh, S.
T5 430-442 Sentence denotes K., Paik, W.
T5 430-442 Sentence denotes K., Paik, W.
T6 443-468 Sentence denotes K., and Kim, S. (1988) J.
T6 443-468 Sentence denotes K., and Kim, S. (1988) J.
T7 469-474 Sentence denotes Biol.
T7 469-474 Sentence denotes Biol.
T8 475-480 Sentence denotes Chem.
T8 475-480 Sentence denotes Chem.
T9 481-499 Sentence denotes 263, 19024-19033).
T9 481-499 Sentence denotes 263, 19024-19033).
T10 500-897 Sentence denotes In the present study, however, we report that heterogeneous ribonucleoprotein particle protein A1 is most likely an in vivo substrate for the "histone-specific protein methylase I." The unmethylated recombinant protein A1 has been found to be a much superior methyl acceptor for the enzyme than histone with a Km value two orders of magnitude lower (0.19 microM) than that for histone (21 microM).
T10 500-897 Sentence denotes In the present study, however, we report that heterogeneous ribonucleoprotein particle protein A1 is most likely an in vivo substrate for the "histone-specific protein methylase I." The unmethylated recombinant protein A1 has been found to be a much superior methyl acceptor for the enzyme than histone with a Km value two orders of magnitude lower (0.19 microM) than that for histone (21 microM).
T11 898-1170 Sentence denotes Myelin basic protein, a specific inhibitor for histone protein methylase I, exhibited a lower IC50 for protein A1 methylation (IC50 = 33 microM) compared with histone methylation (IC50 = 220 microM) and competitively inhibited the former with a Ki value of 1.3 x 10(-6) M.
T11 898-1170 Sentence denotes Myelin basic protein, a specific inhibitor for histone protein methylase I, exhibited a lower IC50 for protein A1 methylation (IC50 = 33 microM) compared with histone methylation (IC50 = 220 microM) and competitively inhibited the former with a Ki value of 1.3 x 10(-6) M.
T12 1171-1333 Sentence denotes The extent of inhibition of protein A1 and histone methylation by the polyclonal antibodies prepared against purified "histone protein methylase I" was identical.
T12 1171-1333 Sentence denotes The extent of inhibition of protein A1 and histone methylation by the polyclonal antibodies prepared against purified "histone protein methylase I" was identical.
T13 1334-1481 Sentence denotes Maximally, 1.08-mol methyl groups were incorporated per mol of protein A1, which was 27-fold higher than that of histone (0.04 mol/mol of histone).
T13 1334-1481 Sentence denotes Maximally, 1.08-mol methyl groups were incorporated per mol of protein A1, which was 27-fold higher than that of histone (0.04 mol/mol of histone).
T14 1482-1637 Sentence denotes HPLC analysis of the enzymatically methylated amino acid residues in protein A1 revealed the formation of NG-monomethylarginine and NG,NG-dimethylarginine.
T14 1482-1637 Sentence denotes HPLC analysis of the enzymatically methylated amino acid residues in protein A1 revealed the formation of NG-monomethylarginine and NG,NG-dimethylarginine.
T15 1638-1794 Sentence denotes The ratio of NG,NG-dimethylarginine/NG-monomethylarginine increased as a function of incubation period; however, NG,N'G-dimethylarginine was not detectable.
T15 1638-1794 Sentence denotes The ratio of NG,NG-dimethylarginine/NG-monomethylarginine increased as a function of incubation period; however, NG,N'G-dimethylarginine was not detectable.
T16 1795-2088 Sentence denotes Proteolytic cleavage of the methyl-3H-labeled recombinant protein A1 by trypsin and Staphylococcus aureus V8 endoprotease indicated that protein A1 possesses multiple sites for methylation, one of which was identified as residue 194 arginine, which coincided with the in vivo methylation site.
T16 1795-2088 Sentence denotes Proteolytic cleavage of the methyl-3H-labeled recombinant protein A1 by trypsin and Staphylococcus aureus V8 endoprotease indicated that protein A1 possesses multiple sites for methylation, one of which was identified as residue 194 arginine, which coincided with the in vivo methylation site.