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.

Solid-phase luminescent catalyst immunoassay for human serum albumin with hemin as labeling catalyst

1984 ◽  
Vol 156 ◽  
pp. 245-252 ◽  
Author(s):  
Yoshihito Ikariyama ◽  
Shuichi Suzuki ◽  
Masuo Aizawa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solid Phase

At very low concentrations known chaotropes act as kosmotropes for the N and B isoforms of human serum albumin

2013 ◽  
Vol 91 (2) ◽  
pp. 72-78 ◽  
Author(s):  
Priyankar Sen ◽  
Mohd Moin Khan ◽  
Asif Equbal ◽  
Ejaz Ahmad ◽  
Rizwan Hasan Khan
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interaction ◽  
Tertiary Structure ◽  
Guanidine Hydrochloride ◽  
Micelle Formation ◽  
Low Concentrations ◽  
Secondary And Tertiary Structure

Very few studies have been done to understand the effect of millimolar concentrations of chaotropes on protein structure. In our previous study we observed that the secondary and tertiary structure of human serum albumin (HSA) increases in the presence of 5 mmol/L urea. Micelle formation in amphoteric detergents increases in the presence of equivalent concentrations of urea. Here, we observed a significant increase in the secondary and tertiary structure of HSA. Interestingly, guanidine hydrochloride, another chaotropic agent, also shows a similar effect. Our results show electrostatic interaction may play a role in neutral to basic transition in HSA. This study further supports the claim that at millimolar concentrations the chaotropes may act as kosmotropes for proteins.

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

Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubin

1987 ◽  
Vol 65 (8) ◽  
pp. 1927-1934 ◽  
Author(s):  
M. Bouvier ◽  
G. R. Brown ◽  
L. E. St-Pierre
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Phosphate Buffer Solution ◽  
Binding Constants ◽  
Buffer Solution ◽  
A Site ◽  
Scatchard Plots

Strategic peptide sequences, patterned on the sequence 136–148 of the primary structure of human serum albumin, have been immobilized on a cross-linked polyacrylamide support using the solid phase peptide synthesis technique. Certain of the resulting materials proved to be efficient adsorbents for bilirubin from aqueous phosphate buffer solution. Amino acids such as lysine and arginine favour the binding of the ligand, whereas glutamic acid reduces it markedly. From Scatchard plots, first and second equilibrium binding constants, in the range of (0.3–9.6) × 104 M−1, were obtained using a site treatment. These binding constants are comparable to that for the binding of bilirubin by a larger fragment of bovine serum albumin that contains the synthesized sequence.

Sign in / Sign up

Export Citation Format

Share Document