A red-NIR emissive probe for the selective detection of albumin in urine samples and live cells

2017 ◽  
Vol 15 (7) ◽  
pp. 1584-1588 ◽  
Author(s):  
K. Rajasekhar ◽  
Chaithra J. Achar ◽  
Thimmaiah Govindaraju
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Fluorescence Probe ◽  
Urine Samples ◽  
Live Cells ◽  
Selective Detection ◽  
Nir Fluorescence ◽  
Emissive Probe

A red-NIR fluorescence probe (TG-SA) has been designed, synthesised and its utility is demonstrated for staining human serum albumin (HSA) in gel electrophoresis, quantification of HSA in clinical urine samples and monitoring serum albumin homeostasis in live cells.

Extrinsic fluorescence probe study of human serum albumin using Nile red

1996 ◽  
Vol 6 (1) ◽  
pp. 23-32 ◽  
Author(s):  
Daniel M. Davis ◽  
David J. S. Birch
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Probe ◽  
Nile Red

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.

scholarly journals The effect of ligand presaturation on the interaction of serum albumins with an immobilized Cibacron Blue 3G-A studied by affinity gel electrophoresis

1981 ◽  
Vol 199 (3) ◽  
pp. 465-472 ◽  
Author(s):  
E C Metcalf ◽  
B Crow ◽  
P D G Dean
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Dissociation Constant ◽  
Gel Electrophoresis ◽  
Dissociation Constants ◽  
Serum Albumins ◽  
Albumin Ratio ◽  
Cibacron Blue ◽  
Affinity Gel Electrophoresis

The interaction of the immobilized triazine dye Cibacron Blue 3G-A with rat, rabbit, sheep, goat, bovine and human serum albumins was studied by affinity gel electrophoresis. Dissociation constants were estimated in each instance and showed human serum albumin to have a significantly higher affinity for the dye than did albumin from any other species. Pretreatment of the defatted proteins with bilirubin (3 mol of bilirubin/mol of protein) did not increase the dissociation constants of the serum albumins, whereas pretreatment with palmitate (7 mol of palmitate/mol of protein) increased the dissociation constant in all cases: 3-fold for human serum albumin, 15-fold for other serum albumins. Increasing the bilirubin/albumin ratio (to 7:1) did not affect the dissociation constant of the albumins studied. Decreasing the palmitate/albumin ratio decreased the dissociation constant for human serum albumin, but did not affect those of bovine and rat albumins. Altering the chain length of the presaturating fatty acid dramatically changed the dissociation constant of both human and bovine serum albumins. Butyrate, hexanoate, octanoate and decanoate did not significantly influence the dissociation constants of bovine and human serum albumins for Cibacron Blue, whereas laurate, myristate and palmitate greatly increased the dissociation constant. These data are discussed in relationship to the behaviour of albumins during dye--agarose column chromatography. In Addendum the effect of nucleotide presaturation on the interaction between Bacillus stearothermophilus 6-phosphogluconate dehydrogenase and the immobilized triazine dyes Cibacron Blue 3G-A and Procion Red HE-3B was examined, and the implications for dye--ligand chromatography are discussed.

Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

1995 ◽  
Vol 16 (1) ◽  
pp. 851-853 ◽  
Author(s):  
Barbara Marzocchi ◽  
Barbara Magi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

scholarly journals Chemiluminescence lateral flow immunoassay cartridge with integrated amorphous silicon photosensors array for human serum albumin detection in urine samples

2016 ◽  
Vol 408 (30) ◽  
pp. 8869-8879 ◽  
Author(s):  
Martina Zangheri ◽  
Fabio Di Nardo ◽  
Mara Mirasoli ◽  
Laura Anfossi ◽  
Augusto Nascetti ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amorphous Silicon ◽  
Lateral Flow ◽  
Urine Samples ◽  
Lateral Flow Immunoassay

A novel hydrazide Schiff base self-assembled nanoprobe for selective detection of human serum albumin and its applications in renal disease surveillance

2020 ◽  
Vol 8 (36) ◽  
pp. 8346-8355
Author(s):  
Zhi-Gang Wang ◽  
Xiao-Jing Yan ◽  
Hai-Bo Liu ◽  
De-Long Zhang ◽  
Wei Liu ◽  
...  
Keyword(s):  
Schiff Base ◽  
Human Serum Albumin ◽  
Renal Disease ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescent Probe ◽  
Disease Surveillance ◽  
Selective Detection ◽  
Binding Mechanism ◽  
Site Binding

A novel fluorescent probe based on disassembly-induced emission and the site-binding mechanism for HSA detection and applications in renal disease surveillance.

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