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Methods of measurement of the protein glycation products formed in human organism

100%

Staniszewska M. , Gamian A.

nr 4

359-368

The advanced glycation end-products (AGEs) are the compounds formed and accumulated in the organism. There is heterogenous group of the glycation products, which have great variety of structural and functional properties. The glycation end-products can be used as markers of the glycation process. Because of the great heterogeneity of the AGEs there is no specific test for their adequate measurement. In this paper there are presented the chromatographic, colorimetric, spectroscopic, mass-spectrometric and serological methods, which are used for determination of AGEs in biological samples. New procedures for the preparation of the model AGEs have been also described. Special attention has been paid to the immunochemical tests. For further assays the model AGE antigens have to be prepared.

Glyco-centres of Faba bean globulins as a source of epitops

100%

Kostyra H. , Kostyra E. , Krawczuk S. , Jarmolowska B.

nr 3

202-207

The reaction of non-enzymatic glycation of Faba bean globulins progressed effectively in weakly basic medium. The cross-linking of globulins was formed first of all in the results of Schiff?s reaction between aine group of Lys and aldehyde group of glucose. The glycated globulins demonstrated higher immunogenic activity in comparison with the non-glycated ones. This means that non-enzymatic glycation of Faba bean globulins caused the formation of new epitops in the pepide chains. The results achieved prove that non-enzymatic glycation of Faba bean globulins changes their immunogenic properties.

Advanced glycation end-products prepared in solution under high pressure contain epitopes distinct from those formed in the dry reaction at high temperature

100%

Staniszewska M. , Jarosz J. , Jon M. , Gamian A.

tom 53

nr 1

71-78

Advanced glycation end-products play an important role in diseases related to diabetes and aging processes. Model compounds are synthesized in order to prepare the diagnostic and experimental tools for studying the mechanisms of pathogenesis. The objective of the present study was to accelerate glycation and upgrade its efficiency under high-pressure conditions.Aqueous solutions of proteins were kept with carbohydrates under a pressure of up to 850 MPa for several hours. Then the high-pressure glycation (HPG) products were fractionated on a Sephadex G-200 column and characterized with SDS-PAGE and MALDI-TOF mass spectrometry. The low-molecular-mass fraction of glycated proteins was separated from the two fractions containing high- and intermediate-molecular-mass cross-linked products of glycation. The products were then compared with those obtained with the high-temperature glycation (HTG) procedure carried out in dry conditions with a lyophilized mixture of substrates. The fractionated products were used to prepare rabbit sera. The immunoblotting experiments showed that the epitopes on the cross-linked glycation products formed in solution under high pressure differed from those originating in dry conditions at high temperature. Sera against the HPG products were specific to homologous material and did not interact with the fractions obtained by HTG. The antibodies against HTG products recognized HTG but not HPG products.

Biochemical properties and clinical effects of the products formed during the glycation of proteins

88%

Staniszewska M. , Gamian A.

nr 2

123-147

Advanced glycation end-products (AGEs) are formed during non-enzymatic glycation - the process occurring in vitro and in the organism. The glycation products accumulate in tissues and interact with specific receptors, what induces various cellular responses. Some enzymes important in metabolism can be also glycated. The disturbances of homeostasis, related to the glycation products, are the reason for complications observed in diabetes and aging processes. There are presented in this paper: mechanism of the formation of AGEs, their cellular receptor (RAGE), as well as the effects of glycation in aging, diabetes and Alzheimer disease. Finally, there are described the compounds which could be useful as inhibitors of glycation in clinical practice.