Results 171 to 180 of about 19,474 (199)

Glycation of Human Serum Albumin in Diabetes: Impacts on the Structure and Function

Current Medicinal Chemistry, 2014
Diabetes mellitus is one of the most serious diseases in the world. The levels of glycated proteins in the blood of diabetics are higher than that of non-diabetic subjects. The glycation of proteins is believed to link to the occurrence of diabetic complications and related diseases.
Hui, Cao, Tingting, Chen, Yujun, Shi
openaire   +2 more sources

In vitro glycation of human serum albumin by dihydroxyacetone and dihydroxyacetone phosphate

Biochemical and Biophysical Research Communications, 2012
Amino groups in proteins can non-enzymatically react with reducing sugars to generate a structurally diverse group of compounds referred to as advanced glycation end products (AGEs). The in vivo formation of AGEs contributes to some of the complications of diabetes including atherosclerosis, cataract formation, and renal failure.
Seneviratne, Champika, Dombi, G. W., Liu, W., Dain, J. A.   +3 more
openaire   +3 more sources

Characterization of the Glycation of Albumin in Freeze-Dried and Frozen Human Serum

Analytical Chemistry, 1997
Human serum albumin (HSA) in fresh frozen and freeze-dried serum reference materials was examined by mass spectrometry and a variety of affinity chromatography techniques. The relative molecular mass distribution of HSA in fresh frozen serum was found to be identical to that of an HSA standard.
openaire   +2 more sources

Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin

Biochemistry (Moscow), 2007
Glycated human serum albumin (HSA) is known to be involved in the pathogenesis of several diseases, and we have therefore investigated possible alterations in HSA on glycation. HSA was incubated for 5 and 20 weeks independently with constant glucose concentration at 37 degrees C under aerobic conditions. Biochemical, spectral, electrophoretic, circular
Mohd Wajid Ali, Khan, Zafar, Rasheed, Wahid Ali, Khan, Rashid, Ali   +3 more
openaire   +2 more sources

Multispectroscopic studies of the interaction of folic acid with glycated human serum albumin

Journal of Biomolecular Structure and Dynamics, 2018
The interaction between glycated human serum albumin (gHSA) and folic acid (FA) was investigated by various spectroscopic techniques, such as fluorescence, circular dichroism, UV-vis absorption spectroscopy and electrophoretic light scattering technique. These methods characterize the binding properties of an albumin-folic acid system.
Urszula, Śliwińska-Hill, Katarzyna, Wiglusz   +1 more
openaire   +3 more sources

Effect of glycation on human serum albumin–zinc interaction: a biophysical study

JBIC Journal of Biological Inorganic Chemistry, 2018
Zinc deficiency is common in diabetes. However, the cause of this phenomenon is largely unknown. 80% of the absorbed zinc is transported through the blood in association with human serum albumin (HSA). Under persistent hyperglycemia, HSA frequently undergoes non-enzymatic glycation which can affect its structure and metal-binding function.
Sarah, Iqbal, Faizan Abul, Qais, Md Maroof, Alam, Imrana, Naseem   +3 more
openaire   +2 more sources

Detergency effects of nanofibrillar amyloid formation on glycation of human serum albumin

Carbohydrate Research, 2008
The prolonged glycation of human serum albumin (HSA) results in significant changes in its structure. The identity of these structural changes and the influence of carbohydrates on these changes require further study. Here, we evaluated structural changes and amyloid formation of HSA upon incubation with Glc, Fru, or Rib. Fluorescence spectrophotometry,
Naghmeh, Sattarahmady, Ali A, Moosavi-Movahedi, Mehran, Habibi-Rezaei, Shahin, Ahmadian, Ali A, Saboury, Hossein, Heli, Nader, Sheibani   +6 more
openaire   +2 more sources

The effect of full glycation on structure and function of human serum albumin

Journal of Biomolecular Structure and Dynamics
Human serum albumin (HSA) is the most abundant protein carrier found in blood. The level of glycated human serum albumin (GHSA) can be used as a diabetes biomarker. Therefore, many attempts have been made to design selective GHSA detection methods. GHSA has been found to show unique characteristics.
Prin Tadawattana, Sirin Sittiwanichai, Deanpen Japrung, Prapasiri Pongprayoon   +3 more
openaire   +2 more sources

Identification and relative quantification of specific glycation sites in human serum albumin

Analytical and Bioanalytical Chemistry, 2010
Glycation (or non-enzymatic glycosylation) is a common non-enzymatic covalent modification of human proteins. Glucose, the highest concentrated monosaccharide in blood, can reversibly react with amino groups of proteins to form Schiff bases that can rearrange to form relatively stable Amadori products.
Andrej, Frolov, Ralf, Hoffmann
openaire   +2 more sources

Glycation ratio determination through simultaneous detection of human serum albumin and glycated albumin on an advanced lateral flow immunoassay sensor

Lab on a Chip, 2020
We developed two advanced lateral flow immunoassays (LFIAs) for the simultaneous determination of total human serum albumin and glycated albumin concentrations with wide detection ranges and improved glycated albumin selectivity.
Hangil Ki, Jusung Oh, Gyeo-Re Han, Min-Gon Kim   +3 more
openaire   +2 more sources