guanosine-monophosphate and glycyl-histidyl-lysine

guanosine-monophosphate has been researched along with glycyl-histidyl-lysine* in 1 studies

Other Studies

1 other study(ies) available for guanosine-monophosphate and glycyl-histidyl-lysine

Article	Year
NMR studies on binary and ternary Pd(II) complexes formed by the growth-modulating tripeptide glycylhistidyllysine and nucleotides. Journal of inorganic biochemistry, 1987, Volume: 30, Issue:3 The mechanism of transport of Pt(II) and Pd(II) into tissues through blood and that of their elimination in kidney is incompletely known so far. In this respect, the binding of palladium by the tripeptide glycyl-L-histidyl-L-lysine (GHL), a constituent of the human plasma, as a binary complex, and by the nucleotides 5'-IMP and 5'-GMP, as ternary complexes, has been studied by 1H and 13C NMR spectroscopy. These studies have been conducted in aqueous media and at different ligand/metal ratios. At acidic pH, resonances were observed for binary and ternary kinetically stable complexes, and binding sites in these complexes were identified by the effect of binding on chemical shifts of protons and carbon resonances. From these data, stoichiometries and structures of these complexes were proposed. Topics: Growth Substances; Guanine Nucleotides; Guanosine Monophosphate; Humans; Inosine Monophosphate; Inosine Nucleotides; Magnetic Resonance Spectroscopy; Oligopeptides; Palladium; Protein Binding; Protein Conformation	1987

Article

Year

NMR studies on binary and ternary Pd(II) complexes formed by the growth-modulating tripeptide glycylhistidyllysine and nucleotides.

Journal of inorganic biochemistry, 1987, Volume: 30, Issue:3

The mechanism of transport of Pt(II) and Pd(II) into tissues through blood and that of their elimination in kidney is incompletely known so far. In this respect, the binding of palladium by the tripeptide glycyl-L-histidyl-L-lysine (GHL), a constituent of the human plasma, as a binary complex, and by the nucleotides 5'-IMP and 5'-GMP, as ternary complexes, has been studied by 1H and 13C NMR spectroscopy. These studies have been conducted in aqueous media and at different ligand/metal ratios. At acidic pH, resonances were observed for binary and ternary kinetically stable complexes, and binding sites in these complexes were identified by the effect of binding on chemical shifts of protons and carbon resonances. From these data, stoichiometries and structures of these complexes were proposed.

Topics: Growth Substances; Guanine Nucleotides; Guanosine Monophosphate; Humans; Inosine Monophosphate; Inosine Nucleotides; Magnetic Resonance Spectroscopy; Oligopeptides; Palladium; Protein Binding; Protein Conformation

1987