Evaluation of human serum albumin cobalt binding assay for the assessment of myocardial ischemia and myocardial infarction

2004 ◽  
Vol 43 (5) ◽  
pp. 679-680
Author(s):  
N. Handly
Keyword(s):  
Myocardial Infarction ◽  
Human Serum Albumin ◽  
Myocardial Ischemia ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Assay ◽  
Cobalt Binding

Use of Lucifer Yellow VS as a Label in Fluorescent Immunoassays Illustrated by the Determination of Albumin in Serum

1983 ◽  
Vol 20 (4) ◽  
pp. 213-216 ◽  
Author(s):  
M Philip Bailey ◽  
Bernard F Rocks ◽  
Clifford Riley
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Assay ◽  
Lucifer Yellow ◽  
Stokes Shift ◽  
Covalent Bonds ◽  
Mild Conditions ◽  
Sulphydryl Groups

The use of a new label for fluoroimmunoassay is described. Lucifer yellow VS is a highly fluorescent vinyl sulphone dye which, under mild conditions, forms covalent bonds with amino and sulphydryl groups but is extremely stable in water. A large Stokes shift (110 nm) and an emission maximum at 540 nm give Lucifer yellow further advantages over the more commonly used labels. The use of the dye as a label has been demonstrated by developing a heterogeneous fluoroimmunoassay for human serum albumin. The fluoroimmunoassay gave comparable results to those obtained using a less specific colorimetric dye-binding assay (r = 0·97, n = 20). The advantages, limitations, and other potential uses of Lucifer yellow are discussed.

Quantitative Binding Assay for Measuring Specific IgG Antibodies to Alpha-Gal Using the Neoglycoprotein Gal-α-1,3-Gal-β-1,4-Glcnac-Human Serum Albumin

2015 ◽  
Vol 135 (2) ◽  
pp. AB188
Author(s):  
Alexander J. Schuyler ◽  
Hayley R. James ◽  
Theo Rispens ◽  
Lisa J. Workman ◽  
Matthew S. Perzanowski ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Assay ◽  
Igg Antibodies ◽  
Specific Igg ◽  
Specific Igg Antibodies

S-Nitroso Human Serum Albumin Improves Oxygen Metabolism during Reperfusion after Severe Myocardial Ischemia

Pharmacology ◽  
2004 ◽  
Vol 72 (2) ◽  
pp. 106-112 ◽  
Author(s):  
Martin Dworschak ◽  
Maximilian Franz ◽  
Seth Hallström ◽  
Severin Semsroth ◽  
Harald Gasser ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Myocardial Ischemia ◽  
Serum Albumin ◽  
Human Serum ◽  
Oxygen Metabolism

Human serum albumin binding assay based on displacement of a non selective fluorescent inhibitor

2007 ◽  
Vol 17 (16) ◽  
pp. 4646-4649 ◽  
Author(s):  
Atli Thorarensen ◽  
Ronald W. Sarver ◽  
Fang Tian ◽  
Andrea Ho ◽  
Donna L. Romero ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Assay ◽  
Albumin Binding ◽  
Human Serum Albumin Binding

scholarly journals Development of Cobalt-Binding Peptide Chelate from Human Serum Albumin: Cobalt-Binding Properties and Stability

2022 ◽  
Vol 23 (2) ◽  
pp. 719
Author(s):  
Yeonje Cho ◽  
Armin Mirzapour-Kouhdasht ◽  
Hyosuk Yun ◽  
Jeong Hoon Park ◽  
Hye Jung Min ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Terminal Region ◽  
Radioactive Isotopes ◽  
Random Coil ◽  
Binding Property ◽  
Alanine Scanning Mutagenesis ◽  
Cobalt Binding

Radioactive isotopes are used as drugs or contrast agents in the medical field after being conjugated with chelates such as DOTA, NOTA, DTPA, TETA, CyDTA, TRITA, and DPDP. The N-terminal sequence of human serum albumin (HSA) is known as a metal binding site, such as for Co2+, Cu2+, and Ni2+. For this study, we designed and synthesized wAlb12 peptide from the N-terminal region of HSA, which can bind to cobalt, to develop a peptide-based chelate. The wAlb12 with a random coil structure tightly binds to the Co(II) ion. Moreover, the binding property of wAlb12 toward Co(II) was confirmed using various spectroscopic experiments. To identify the binding site of wAlb12, the analogs were synthesized by alanine scanning mutagenesis. Among them, H3A and Ac-wAlb12 did not bind to Co(II). The analysis of the binding regions confirmed that the His3 and α-amino group of the N-terminal region are important for Co(II) binding. The wAlb12 bound to Co(II) with Kd of 75 μM determined by isothermal titration calorimetry when analyzed by a single-site binding model. For the use of wAlb12 as a chelate in humans, its cytotoxicity and stability were investigated. Trypsin stability showed that the wAlb12 − Co(II) complex was more stable than wAlb12 alone. Furthermore, the cell viability analysis showed wAlb12 and wAlb12 + Co(II) to be non-toxic to the Raw 264.7 and HEK 293T cell lines. Therefore, a hot radioactive isotope such as cobalt-57 will have the same effect as a stable isotope cobalt. Accordingly, we expect wAlb12 to be used as a peptide chelate that binds with radioactive isotopes.

scholarly journals Competitive Protein Binding Assay of Naproxen by Human Serum Albumin Functionalized Silicon Dioxide Nanoparticles

Molecules ◽  
2019 ◽  
Vol 24 (14) ◽  
pp. 2593 ◽  
Author(s):  
Qian-Long Wang ◽  
Jing Xie ◽  
Jian Liang ◽  
Geng-Ting Dong ◽  
Li-Sheng Ding ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Silicon Dioxide ◽  
Human Serum ◽  
Binding Assay ◽  
Silicon Dioxide Nanoparticles ◽  
Nano Sio2 ◽  
Protein Binding Assay ◽  
Competitive Protein Binding Assay ◽  
Competitive Protein Binding

We have developed a new competitive protein binding assay (CPBA) based on human serum albumin functionalized silicon dioxide nanoparticles (nano-SiO2-HSA) that can be used for naproxen determination in urine. Compared with a conventional multi-well reaction plate, nano-SiO2 with a high surface-area-to-volume ratio could be introduced as a stationary phase, markedly improving the analytical performance. Nano-SiO2-HSA and horseradish peroxidase-labeled-naproxen (HRP-naproxen) were prepared for the present CPBA method. In this study, a direct competitive binding to nano-SiO2-HSAwas performed between the free naproxen in the sample and HRP-naproxen. Thus, the catalytic color reactions were investigated on an HRP/3,3′5,5′-tetramethylbenzidine (TMB)/H2O2 system by the HRP-naproxen/nano-SiO2-HSA composite for quantitative measurement via an ultraviolet spectrophotometer. A series of validation experiments indicated that our proposed methods can be applied satisfactorily to the determination of naproxen in urine samples. As a proof of principle, the newly developed nano-CPBA method for the quantification of naproxen in urine can be expected to have the advantages of low costs, fast speed, high accuracy, and relatively simple instrument requirements. Our method could be capable of expanding the analytical applications of nanomaterials and of determining other small-molecule compounds from various biological samples.

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