scholarly journals Design of Coelenterazine Analogue to Reveal Bioluminescent Reaction of Human Serum Albumin

2021 ◽  
Author(s):  
Ryo Nishihara ◽  
Kazuki Niwa ◽  
Tatsunosuke Tomita ◽  
Ryoji Kurita
Keyword(s):  
Quantitative Analysis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Alkyl Chain ◽  
Light Emission ◽  
Enzymatic Oxidation ◽  
Luminescence Properties ◽  
Kinetic Properties ◽  
Serum Samples

This chapter describes the design of an imidazopyrazinone-type luciferin named as HuLumino1 by us and investigation of its luminescence properties. This luciferin was designed to generate bioluminescence by human serum albumin (HSA) rather than by luciferase derived from luminous organisms. HuLumino1 was developed by modifying a methoxy-terminated alkyl chain to the C-6 position and eliminating a benzyl group at the C-8 position of coelenterazine. To clarify the basis of light emission by HSA, the detailed kinetic properties of the HuLumino1/HSA pair were investigated using a calibrated luminometer. The enzymatic oxidation of HuLumino1 was observed only in the presence of HSA. Results of HSA quantification experiments using HuLumino1 agreed with less than 5% differences with those of enzyme-linked immunosorbent assays, suggesting HuLumino1 could be used for quantitative analysis of HSA levels in serum samples without any pretreatments. These results demonstrate the advantages of the coelenterazine analogue as a bioluminescence reagent to detect non-labeled proteins, which generally do not function as enzymes.

scholarly journals Gradients of a Sandwich-structured Immunosensor Controlled Using Magnetized Masks for Determination of Human Serum Albumin Using Electrochemiluminescence

2021 ◽  
Author(s):  
Chun-Yao Huang ◽  
Chi-Jung Chang ◽  
Bohr-Ran Huang ◽  
Chien-Hsing Lu ◽  
jemkun chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Magnetic Beads ◽  
Limit Of Detection ◽  
High Reliability ◽  
Water Evaporation ◽  
Serum Samples ◽  
Dry Process ◽  
Physical Features

Abstract Background: Separation of macromolecules or particles from a colloid system to from gradient structure on the surface has been employed for biosensing systems, suggesting an enhancement of the chemical and physical features of particles. Performance of an electrochemiluminescence (ECL) immunosensor was employed to improve with a particle gradient.Results: Magnetic beads with silicon dioxide coating were adopted as nanocarriers for gradient manipulation and immobilized with the primary antibody. Cadmium telluride quantum dots (CdTe QDs) were coated with a layer of protein G for conjugation and orientation of secondary antibody as signal labels. ECL immunosensor gradients upon the electrode were formed by magnetolithography with magnetized nickel masks of column and stripe arrays at various scales. The immunosensor generally aggregated as island on the substrate through a dry process of water evaporation leading to a decrease of efficiency in the characteristic signals. Stripe arrays of magnetized nickel were designed to generate cylindrical magnetic flux on the substrate to improve the particle manipulation with the gradient. Various gradients of the sandwich-structured immunosensor substantially affected the electrochemical performance. Compared to the gradient-free immunosensor, the gradient of the immunosensor generated using the 3-μm-stripe array mask of magnetolithography enhanced the ECL intensity ~2.2 times. Conclusions: The results of quantification of human serum albumin (HSA) with the gradient immunosensor showed a broad linear range (15–420 ng mL−1), a low limit of detection (8 ng mL−1) and high reliability for HSA-spiked serum samples, indicating that the immunosensor gradient substantially enhances the performance of the ECL assay.

Quantitative Analysis of Cysteine-34 On the Anitioxidative Properties of Human Serum Albumin in Hemodialysis Patients

2011 ◽  
Vol 100 (9) ◽  
pp. 3968-3976 ◽  
Author(s):  
Makoto Anraku ◽  
Koji Takeuchi ◽  
Hiroshi Watanabe ◽  
Daisuke Kadowaki ◽  
Kenichiro Kitamura ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Hemodialysis Patients

scholarly journals Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI–TOF MS

2011 ◽  
Vol 412 (17-18) ◽  
pp. 1606-1615 ◽  
Author(s):  
Omar S. Barnaby ◽  
Ronald L. Cerny ◽  
William Clarke ◽  
David S. Hage
Keyword(s):  
Quantitative Analysis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
18O Labeling ◽  
Tof Ms

Bilirubin binding by primary sites of human serum albumin, with suppression of secondary-site interference by use of a high salt concentration.

1980 ◽  
Vol 26 (1) ◽  
pp. 107-110 ◽  
Author(s):  
R B Rutkowski
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Secondary Site ◽  
Serum Samples ◽  
Nacl Concentration ◽  
Spectral Absorbance ◽  
Bilirubin Binding ◽  
Column Procedure ◽  
Site Binding

Abstract A high (2.0 mol/L) NaCl concentration apparently suppresses the secondary-site binding of bilirubin by human serum albumin. Thus if an excess of bilirubin is added to human serum albumin or to neonatal serum in buffer containing 0.1 mol of tris(hydroxymethyl)aminomethane and 2.0 mol of NaCl per liter (pH 7.5), and the bilirubin not bound to albumin is removed by treatment with calcium carbonate, the bilirubin binding reserve of primary binding sites can be estimated from direct measurement of spectral absorbance at 468 nm. Hemolysis and conjugated bilirubin apparently do not interfere. In a comparison study with serum samples from neonates the method gave results that generally agreed with those obtained by a commercially available Sephadex G-25 column procedure. In serum samples from adults the calculated unbound unconjugated bilirubin (free bilirubin) values derived by using binding reserves determined by the proposed method correlated well with the free bilirubin concentrations measured by a peroxidase method, but were only about one-half the amounts obtained by the peroxidase method.

Bilirubin binding by primary sites of human serum albumin, with suppression of secondary-site interference by use of a high salt concentration.

1980 ◽  
Vol 26 (1) ◽  
pp. 107-110
Author(s):  
R B Rutkowski
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Secondary Site ◽  
Serum Samples ◽  
Nacl Concentration ◽  
Spectral Absorbance ◽  
Bilirubin Binding ◽  
Column Procedure ◽  
Site Binding

Abstract A high (2.0 mol/L) NaCl concentration apparently suppresses the secondary-site binding of bilirubin by human serum albumin. Thus if an excess of bilirubin is added to human serum albumin or to neonatal serum in buffer containing 0.1 mol of tris(hydroxymethyl)aminomethane and 2.0 mol of NaCl per liter (pH 7.5), and the bilirubin not bound to albumin is removed by treatment with calcium carbonate, the bilirubin binding reserve of primary binding sites can be estimated from direct measurement of spectral absorbance at 468 nm. Hemolysis and conjugated bilirubin apparently do not interfere. In a comparison study with serum samples from neonates the method gave results that generally agreed with those obtained by a commercially available Sephadex G-25 column procedure. In serum samples from adults the calculated unbound unconjugated bilirubin (free bilirubin) values derived by using binding reserves determined by the proposed method correlated well with the free bilirubin concentrations measured by a peroxidase method, but were only about one-half the amounts obtained by the peroxidase method.

Rhenium tricarbonyl complexes of AIE active tetraarylethylene ligands: tuning luminescence properties and HSA-specific binding

2017 ◽  
Vol 46 (43) ◽  
pp. 15040-15047 ◽  
Author(s):  
Moustafa T. Gabr ◽  
F. Christopher Pigge
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Specific Binding ◽  
Luminescence Properties ◽  
Rhenium Tricarbonyl

A luminescent tetraarylethylene Re(i) bioprobe exhibits enhanced emission upon site II-specific binding to human serum albumin.

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