Journal ArticleDOI
Binding of actinomycin D and divalent cations to lipopolysaccharides ofAgrobacterium tumefaciens as studied by fluorescence spectroscopy
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TLDR
The binding of actinomycin D and divalent cations to lipopolysaccharides of A. tumefaciens was studied and revealed 2 binding sites (low and high affinity sites) for dovalent cations and 1 high-affinity site for actinomecin D.Abstract:
The binding of actinomycin D and divalent cations to lipopolysaccharides ofA. tumefaciens was studied. Fluorimetric titrations revealed 2 binding sites (low and high affinity sites) for divalent cations, and 1 high-affinity site for actinomycin D.read more
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Interaction of Divalent Cations and Polymyxin B With Lipopolysaccharide
Melvin Schindler,M. J. Osborn +1 more
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Sialic acid. A calcium-binding carbohydrate.
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Mechanism of lysozyme catalysis: role of ground-state strain in subsite D in hen egg-white and human lysozymes.
TL;DR: The association constants for the binding of various saccharides to hen egg-white lyso enzyme and human lysozyme have been measured by fluorescence titration and it is suggested that subsite C of the human enzyme is "looser" than the equivalent site in the hen egg enzyme, so that the rearrangement of a saccharide in this subsite in response to introduction of an N-acetylmuramic acid residue into subsite D destabilizes the saccharid complexes
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Assignment of the 13C nuclear magnetic resonance spectrum of aqueous ganglioside GM1 micelles.
TL;DR: It is proposed that the higher affinity, compared with monomeric sialic acid, of GM1 for cations may result from these additional oligosaccharide groups, which may effectively compete for water ligands in the metal cation coordination sphere.