Results 161 to 170 of about 19,474 (199)

Comparative study of thermal domains analyzing of glycated and non-glycated human serum albumin

Thermochimica Acta, 2014
Abstract Protein resistance against denaturant agent is a useful property in industrial applications. In the current research, the domains thermal unfolding of glycated human serum albumin (GHSA) and human serum albumin (HSA) were studied under incubation at physiological conditions for 35 days.
Mousa Bohlooli, Ali Akbar Moosavi-Movahedi, Mansour Ghaffari-Moghaddam   +2 more
exaly   +2 more sources

Glycation of human serum albumin: inhibition by Diclofenac

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
Glycation is a non-enzymatic modification of proteins by sugars, probably responsible for the initiation of complications in diabetes patients and aging individuals. Our in vitro experiments show an inhibition of sugar attachment in the presence of Diclofenac. The levels of advanced glycation products, measured as specific fluorescent groups, were also
M A, van Boekel, P J, van den Bergh, H J, Hoenders   +2 more
openaire   +2 more sources

A study on human serum albumin influence on glycation of fibrinogen

Biochemical and Biophysical Research Communications, 2013
Although in vivo glycation proceeds in complex mixture of proteins, previous studies did not take in consideration the influence of protein-protein interaction on Maillard reaction. The aim of our study was to test the influence of human serum albumin (HSA) on glycation of fibrinogen.
Martyna, Kielmas, Zbigniew, Szewczuk, Piotr, Stefanowicz   +2 more
openaire   +2 more sources

Sensitive Detection of Glycated Albumin in Human Serum Albumin Using Electrochemiluminescence

Analytical Chemistry, 2017
Monitoring of blood glucose content is vital for diabetes patients. The conventional widely used method involves an invasive procedure for blood sampling. In addition, blood glucose measured by this way is affected by immediate food consumption and it does not show accurate baseline blood glucose measurement.
Yuki Inoue, Mikako Inoue, Masato Saito, Hiroyuki Yoshikawa, Eiichi Tamiya   +4 more
openaire   +2 more sources

Glycation Alters the Fatty Acid Binding Capacity of Human Serum Albumin

Journal of Agricultural and Food Chemistry, 2022
Glycation significantly alters the physicochemical and biofunctional properties of proteins in foods and in vivo. In the present study, human serum albumin (HSA) as the major transporter of fatty acids was modified with glyoxal under physiological conditions.
Christian Henning, Christine Stübner, Seyed Hamidreza Arabi, Jörg Reichenwallner, Dariush Hinderberger, Roman Fiedler, Matthias Girndt, Simone Di Sanzo, Alessandro Ori, Marcus A. Glomb   +9 more
openaire   +2 more sources

The effect of non-enzymatic glycation on the unfolding of human serum albumin

Archives of Biochemistry and Biophysics, 2005
We monitored the unfolding of human serum albumin (HSA) and glycated human serum albumin (gHSA) subjected to guanidine hydrochloride (GndHCl) by using fluorescence and circular dichroism (CD) spectroscopy. A two-state model with sloping baselines best described the Trp-214 fluorescence unfolding measurements, while a three-state model best described ...
Deanna L, Mendez, Russell A, Jensen, Laura A, McElroy, Jose M, Pena, Raymond M, Esquerra   +4 more
openaire   +2 more sources

Targeted Quantification of the Glycated Peptides of Human Serum Albumin

2017
Glycated human serum albumin (HSA) serves as an important marker for monitoring the glycemic status. Developing methods for unambiguous identification and quantification of glycated peptides of HSA using high-throughput technologies such as mass spectrometry has a great clinical significance.
Garikapati, Vannuruswamy, Korwar, Arvind M., Jagadeeshaprasad, Mashanipalya G., Kulkarni, Mahesh J., Greening, David W., Simpson, Richard J.   +5 more
openaire   +3 more sources

The in vitro glycation of human serum albumin in the presence of Zn(II)

Journal of Inorganic Biochemistry, 2011
Amino groups of human serum albumin (HSA) can react non-enzymatically with carbonyl groups of reducing sugars to form advanced glycation end products (AGEs). These AGEs contribute to many of the chronic complications of diabetes including atherosclerosis, cataract formation and renal failure.
Champika, Seneviratne, G W, Dombi, W, Liu, J A, Dain   +3 more
openaire   +2 more sources

Effects of glycation on meloxicam binding to human serum albumin

Journal of Molecular Structure, 2011
Abstract The current study reports a binding of meloxicam a pharmacologically important new generation, non-steroidal anti-inflammatory drug to glycated form of the human serum albumin (HSA). The interaction of the meloxicam with nonglycated and glycated albumin has been studied at pH 7.4 in 0.05 M sodium phosphate buffer with 0.1 M NaCl, using ...
Lilianna Trynda-Lemiesz, Katarzyna Wiglusz   +1 more
openaire   +2 more sources

Investigation of thermal reversibility and stability of glycated human serum albumin

International Journal of Biological Macromolecules, 2013
Protein glycation, the process by which carbohydrates attach to proteins upon covalent binding, can alter protein thermal reversibility and stability. Protein stability and reversibility have important role in protein behavior and function. Also they are benefit properties for drug produce and protein industrial applications.
M, Bohlooli, A A, Moosavi-Movahedi, F, Taghavi, P, Maghami, A A, Saboury, Z, Moosavi-Movahedi, M, Farhadi, J, Hong, N, Sheibani, M, Habibi-Rezaei   +9 more
openaire   +2 more sources