Antioxidant capacity and structural changes of human serum albumin from patients in advanced stages of diabetic nephropathy and the effect of the dialysis

2015 ◽  
Vol 404 (1-2) ◽  
pp. 193-201 ◽  
Author(s):  
Marisol Rosas-Díaz ◽  
Menandro Camarillo-Cadena ◽  
Andrés Hernández-Arana ◽  
Eva Ramón-Gallegos ◽  
Rafael Medina-Navarro
Keyword(s):  
Diabetic Nephropathy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Antioxidant Capacity ◽  
Human Serum ◽  
Structural Changes ◽  
Advanced Stages

Rapid detection and initial characterization of genetic variants of human serum albumin

1991 ◽  
Vol 37 (7) ◽  
pp. 1221-1224 ◽  
Author(s):  
J Merle Sheat ◽  
Robert J Peach ◽  
Peter M George
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl

Abstract We have studied the detection and classification of genetic variants of human serum albumin by electrophoresis. Samples from 10 patients who were heterozygous for eight different albumin variants were studied by two methods. In agarose gel electrophoresis, each of these variants has an abnormal mobility and can be classified on the basis that structural changes at the N-terminus abolish 63Ni binding. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole serum, glycosylated variants are easily detected because of their greater apparent molecular mass.

Rapid, competitive enzymoimmunoassay for albumin in urine.

1986 ◽  
Vol 32 (4) ◽  
pp. 669-671 ◽  
Author(s):  
J Chesham ◽  
S W Anderton ◽  
C F Kingdon
Keyword(s):  
Diabetic Nephropathy ◽  
Human Serum Albumin ◽  
Horseradish Peroxidase ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Urine ◽  
Solid Phase ◽  
Low Concentrations ◽  
Initiation Of Therapy ◽  
Assay Protocol

Abstract In this solid-phase competitive enzymoimmunoassay for albumin in human urine, antiserum to human serum albumin labeled with horseradish peroxidase (EC 1.11.1.7) is incubated with solid-phase-bound human serum albumin in the presence of sample or standard. Results obtained correlate well (r = 0.96) with those of an established fluoroimmunoassay. The present assay covers the range 0.9 to 200 mg/L and can be performed within 1 h. These characteristics, together with the simplicity of the assay protocol, make it very useful for monitoring low concentrations of albumin in urine. Detection of such minimal albuminuria allows initiation of therapy that may prevent development of clinical proteinuria and associated diabetic nephropathy.

scholarly journals Polyphenol capping on a gold nanosurface modulates human serum albumin fibrillation

2020 ◽  
Vol 1 (5) ◽  
pp. 1142-1150
Author(s):  
Aalok Basu ◽  
Sonia Kundu ◽  
Aatrayee Das ◽  
Chitra Basu ◽  
Sagar Bhayye ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Antioxidant Capacity ◽  
Human Serum

The antioxidant capacity inherent to polyphenol-capped gold nanoparticles contributed to the inhibition of human serum albumin fibrillation.

Hyperglycemia induced reactive species trigger structural changes in human serum albumin of type 1 diabetic subjects

2018 ◽  
Vol 107 ◽  
pp. 2141-2149 ◽  
Author(s):  
Zarina Arif ◽  
Km Neelofar ◽  
Mir Yasir Arfat ◽  
Asif Zaman ◽  
Akhlas Tarannum ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structural Changes ◽  
Reactive Species

Structural Changes of Human Serum Albumin (HSA) in Simulated Microgravity

2018 ◽  
Vol 24 (11) ◽  
pp. 1030-1039 ◽  
Author(s):  
Azadeh Hekmat ◽  
Zahra Hajebrahimi ◽  
Amir Motamedzade
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structural Changes ◽  
Simulated Microgravity
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