| Autor: |
Pereira Morais MP; Department of Biology and Biochemistry, University of Bath, Bath, UK., Kassaar O; Department of Biology and Biochemistry, University of Bath, Bath, UK., Flower SE; Department of Chemistry, University of Bath, Bath, UK., Williams RJ; Department of Biology and Biochemistry, University of Bath, Bath, UK., James TD; Department of Chemistry, University of Bath, Bath, UK., van den Elsen JMH; Department of Biology and Biochemistry, University of Bath, Bath, UK. J.M.H.V.Elsen@bath.ac.uk. |
| Abstrakt: |
Carbohydrate modification of proteins adds complexity and diversity to the proteome. However, undesired carbohydrate modifications also occur in the form of glycation, which have been implicated in diseases such as diabetes, Alzheimer's disease, autoimmune diseases, and cancer. The analysis of glycated proteins is challenging due to their complexity and variability. Numerous analytical techniques have been developed that require expensive specialized equipment and complex data analysis. In this chapter, we describe two easy-to-use electrophoresis-based methods that will enable researchers to detect, identify, and analyze these posttranslational modifications. This new cost-effective methodology will aid the detection of unwanted glycation products in processed foods and may lead to new diagnostics and therapeutics for age-related chronic diseases. |
