Nonenzymatic glucosylation of human serum albumin and its influence on binding capacity of sulfonylureas.

  title={Nonenzymatic glucosylation of human serum albumin and its influence on binding capacity of sulfonylureas.},
  author={Seishi Tsuchiya and T Sakurai and S Sekiguchi},
  journal={Biochemical pharmacology},
  volume={33 19},

Binding of tolbutamide to glycated human serum albumin.

Chromatographic analysis of acetohexamide binding to glycated human serum albumin.

Influence of glycosylation on the drug binding of human serum albumin.

The results suggested that hydrophobic interaction is the predominant force for the drug binding in HSA, perhaps due to a conformational change or steric hindrance when further glycosylation occurred.

Chromatographic studies of chlorpropamide interactions with normal and glycated human serum albumin based on affinity microcolumns.

Binding properties of glycosylated albumin and acetaldehyde albumin.

The results indicate that prolonged exposure of purified human serum albumin to acetaldehyde results in a major acetaldehyde albumin fraction that lacks the ability to bind MADDS and diazepam, and suggests that altered drug binding in alcoholics may be partially explained by altered binding ability of acetaldehydealbumins.

Lactosylation of albumin reduces uptake rate of dibromosulfophthalein in perfused rat liver and dissociation rate from albumin In Vitro

The decreased off‐rate from lactosylated albumin can explain the retarding influence on hepatic uptake rate of dibromosulfophthalein, and argues for the concept of dissociation‐limited uptake in the hepatic clearance of the organic anion.

Calcium ion binding to clinically relevant chemical modifications of human serum albumin.

A finding showing that the thiol group of cysteine 34 is not important for calcium binding is shown, and the enhancement of binding resulting from glycation or penicilloylation is probably brought about by unspecific electrostatic effects, possibly supplemented by conformational changes of the protein molecule.



Glucosylated albumin and its influence on salicylate binding.

The results indicated that glucose reacted with albumin by a nonenzymatic process involving Schiff base formation and Amadori rearrangement to a stable ketoamine derivative.

Binding of sulfonylureas to serum proteins.

  • J. Judis
  • Chemistry, Medicine
    Journal of pharmaceutical sciences
  • 1972
Inhibition of protein (albumin) binding of the sulfonylureas by drugs known to potentiate their action was studied and binding of tolbutamide was inhibited by sulfaphenazole and phenylbutazone most markedly and somewhat less by sodium salicylate, aspirin, sulfadimethoxine, and sulfisoxazole.

The binding of sulphonylureas to serum albumin

Binding parameters corrected for electrostatic effects were found to fit binding data for tolbutamide, chlorpropamide and tolazamide better than uncorrected parameters, implying that the predominantly bound species is the anion.

Inactivation of bovine kidney beta-N-acetyl-D-glucosaminidase by nonenzymatic glucosylation.

Evidence is presented that the incubation of beta-N-acetyl-D-glucosaminidase from bovine kidney with glucose leads to the covalent incorporation of the sugar into the enzyme protein, and the possibility that nonenzymatic glucosylation of the enzyme might occur in vivo is considered.

The glycosylation of hemoglobin: relevance to diabetes mellitus.

By providing an integrated measurement of blood glucose, hemoglobin AIc is useful in assessing the degree of diabetic control and is a useful model of nonenzymatic glycosylation of other proteins that may be involved in the long-term complications of the disease.