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Journal ArticleDOI

Glucose modification of human serum albumin: a structural study.

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TLDR
Structural changes associated with the exposure of human serum albumin to glucose with or without the presence of Cu (II) have been characterized using a bank of methods for structural analysis including circular dichroism, amino acid analysis, fluorescence measurements, SDS-PAGE, and boronate binding.
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This article is published in Free Radical Biology and Medicine.The article was published on 1997-01-01. It has received 108 citations till now. The article focuses on the topics: Glycation & Amadori rearrangement.

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Citations
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Human serum albumin: from bench to bedside.

TL;DR: HSA is a valuable biomarker of many diseases, including cancer, rheumatoid arthritis, ischemia, post-menopausal obesity, severe acute graft-versus-host disease, and diseases that need monitoring of the glycemic control.
Journal ArticleDOI

The glycation of albumin: Structural and functional impacts

TL;DR: The impact of glycation on the structure of albumin and its various activities, especially its antioxidant and binding capacities is reported, specifically the role of the protein as a biological marker of diabetes.
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Chelating activity of advanced glycation end-product inhibitors.

TL;DR: Inhibition of AGE formation results primarily from the chelating or antioxidant activity of the AGE inhibitors, rather than their carbonyl trapping activity.
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Glucose and free radicals impair the antioxidant properties of serum albumin

TL;DR: It is proposed that, considering the poor glucose control found in diabetics as well as the key role of oxidative stress in vascular complications, glycation‐mediated and free radical‐induced impairment of the antioxidant properties of albumin might be important parameters in vascular complication encountered in diabetes.
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Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics

TL;DR: A set of parameters are proposed that are sufficient to partially characterize AGEs used for biochemical studies and suggest strong conformational changes within the modified proteins.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
PatentDOI

Measurement of protein using bicinchoninic acid

TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.
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Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels

TL;DR: A new modification of silver staining is presented which utilizes two chemical properties of thiosulfate: image enhancement by pretreatment of fixed gels, and formation of soluble silver complexes which prevents unspecific background staining during image development.
Journal ArticleDOI

Atomic structure and chemistry of human serum albumin.

TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.