1H NMR investigation of the binding of methyl-beta-D-galactoses with sialic acid residues on hepatic binding protein--the effect of divalent calcium ions.
The present study is a proton NMR investigation of the influence of Ca2+ on the interaction between the intact sialic acid residues on HBP (Hepatic Binding Protein) and methyl-beta-D-galactoses. The proton NMR spectra of HBP and methyl-beta-D-galactose mixing solution at different Ca2+ concentration have been measured. The analysis of the experimental results indicates that Ca2+ participates in the binding of sialic acid residues on HBP with methyl-beta-D-galactoses and this enables the galactose molecules to be in stable bound state. The proton NMR spectra of the samples containing EDTA have confirmed this conclusion.
D000818:Animals; D037263:Asialoglycoprotein Receptor; D002118:Calcium / Q000494:pharmacology*; D002352:Carrier Proteins / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008756:Methylgalactosides / Q000378:metabolism*; D008759:Methylglycosides / Q000378:metabolism*; D011817:Rabbits; D012794:Sialic Acids / Q000378:metabolism*
D037263:Asialoglycoprotein Receptor; D002352:Carrier Proteins; D008756:Methylgalactosides; D008759:Methylglycosides; D012794:Sialic Acids; C027122:hepatic sialoglycoprotein receptor; D002118:Calcium; D005690:Galactose