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 ◽  
Vol 20 (4) ◽  
pp. 844-851 ◽  
Author(s):  
Hangil Ki ◽  
Jusung Oh ◽  
Gyeo-Re Han ◽  
Min-Gon Kim

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.

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko

Biothiols are extremely powerful antioxidants that protect cells against the effects of oxidative stress. They are also considered relevant disease biomarkers, specifically risk factors for cardiovascular disease. In this paper, a new procedure for the simultaneous determination of human serum albumin and low-molecular-weight thiols in plasma is described. The method is based on the pre-column derivatization of analytes with a thiol-specific fluorescence labeling reagent, monobromobimane, followed by separation and quantification through reversed-phase high-performance liquid chromatography with fluorescence detection (excitation, 378 nm; emission, 492 nm). Prior to the derivatization step, the oxidized thiols are converted to their reduced forms by reductive cleavage with sodium borohydride. Linearity in the detector response for total thiols was observed in the following ranges: 1.76–30.0 mg mL−1 for human serum albumin, 0.29–5.0 nmol mL−1 for α-lipoic acid, 1.16–35 nmol mL−1 for glutathione, 9.83–450.0 nmol mL−1 for cysteine, 0.55–40.0 nmol mL−1 for homocysteine, 0.34–50.0 nmol mL−1 for N-acetyl-L-cysteine, and 1.45–45.0 nmol mL−1 for cysteinylglycine. Recovery values of 85.16–119.48% were recorded for all the analytes. The developed method is sensitive, repeatable, and linear within the expected ranges of total thiols. The devised procedure can be applied to plasma samples to monitor biochemical processes in various pathophysiological states.


Talanta ◽  
2016 ◽  
Vol 154 ◽  
pp. 341-345 ◽  
Author(s):  
Hong-Bing Duan ◽  
Jun-Tao Cao ◽  
Jiu-Jun Yang ◽  
Hui Wang ◽  
Yan-Ming Liu

2016 ◽  
Vol 408 (30) ◽  
pp. 8869-8879 ◽  
Author(s):  
Martina Zangheri ◽  
Fabio Di Nardo ◽  
Mara Mirasoli ◽  
Laura Anfossi ◽  
Augusto Nascetti ◽  
...  

1998 ◽  
Vol 44 (2) ◽  
pp. 256-263 ◽  
Author(s):  
Kazuyoshi Ikeda ◽  
Yuichiro Sakamoto ◽  
Yukie Kawasaki ◽  
Takehiro Miyake ◽  
Kimikazu Tanaka ◽  
...  

Abstract A new affinity method for quantification of glycated albumin by an enzyme-linked boronate-immunoassay (ELBIA) has been established, based on the interaction between boronic acids and the cis-diols of glycated human serum albumin (HSA) trapped by anti-HSA antibody. To evaluate the ELBIA, we first examined the accuracy of the conventional boronate affinity chromatographic (BAC) method. In the BAC method, 8.1–18.9% of nonglycated albumin calibrator nonspecifically bound to the boronate affinity column, values that were regarded as the column blank. In the modified BAC method, therefore, we subtracted the column blank value from the measured glycated albumin value to obtain the true value. Because glycated albumin values measured by ELBIA were exactly the same as reported by the modified BAC method, we suggest that the ELBIA results reflect the real status of albumin glycation. We have also developed a fully automated ELBIA system, allowing multiple, rapid, and precise measurements of glycated albumin.


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