Characterization of binary solvent mixtures
Explore the source record for details and available documents.
Journal Article↗
Biomedical subjects
F Garcia-Blanco
Publications and source records attributed to F Garcia-Blanco.
Thermodynamic analysis of the interaction of the antibiotic teicoplanin and its aglycone with cell-wall peptides.
The thermodynamics of the interaction of the glycopeptidic antibiotic teicoplanin and its peptidic moiety with analogues of bacterial cell-wall peptides were studied by means of calorimetric and spectrophotometric techniques. The analysis of the thermodynamic data has allowed us to evaluate the contributions of the different peptide groups to the binding process. The nature of the primary binding forces is also discussed for each interacting group, on the basis of their enthalpic and entropic contribution and in connection with the detailed structural information available for these antibiotics from n.m.r. data. Similar analyses for the case of vancomycin and ristocetin are also reported.
Amino Acid Sequence↗
Studies on the pyridoxal phosphate site in glycogen phosphorylase b.
It is usually accepted that the adduct formed by reaction of pyridoxal phosphate with amines in aprotic solvents is a good model to stimulate some properties of the pyridoxal phosphate site in glycogen phosphorylase. The chemical structure of this adduct was not very well established. An aldimine structure is supported by the infrared, electronic absorption and nuclear magnetic resonance spectra given in this work. Therefore, we conclude that, at neutral pH, the pyridoxal phosphate is bound to the glycogen phosphorylase through a Schiff base structure and embedded in a hydrophobic environment. The polarographic measurements reported in this paper could explain the fact that, at neutral pH, the pyridoxal phosphate can not be reduced onto phosphorylase by NaBH4.
Binding Sites↗