Determination of gamma-globulin at nanogram levels by its quenching effect on the fluorescence of a red emitting conjugated polymer

2015 ◽  
Vol 39 (6) ◽  
pp. 4551-4555 ◽  
Author(s):  
Ping Zhang ◽  
Shujuan Zhuo ◽  
Lilin Sun ◽  
Ping Zhang ◽  
Changqing Zhu
Keyword(s):  
Serum Albumin ◽  
Conjugated Polymer ◽  
Gamma Globulin ◽  
Fluorescence Sensor ◽  
Quenching Effect

A novel red emitting fluorescence sensor has been constructed and used for the selective assay of gamma-globulin in the presence of serum albumin.

A label-free conjugated polymer-based fluorescence assay for the determination of adenosine triphosphate and alkaline phosphatase

2014 ◽  
Vol 38 (9) ◽  
pp. 4574-4579 ◽  
Author(s):  
Yanan Li ◽  
Yan Li ◽  
Xinyan Wang ◽  
Xingguang Su
Keyword(s):  
Alkaline Phosphatase ◽  
Adenosine Triphosphate ◽  
Conjugated Polymer ◽  
Fluorescence Assay ◽  
Label Free ◽  
Quenching Effect ◽  
Hydrolysis Of

A sensor was developed based on the quenching effect of Cu2+ on PPESO3 and the hydrolysis of ATP by ALP.

scholarly journals Simultaneous Determination of Human Serum Albumin and Low-Molecular-Weight Thiols after Derivatization with Monobromobimane

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Simultaneous Determination ◽  
Reversed Phase ◽  
Fluorescence Labeling ◽  
Detector Response ◽  
Low Molecular Weight

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.

Comparison of several methods for semiquantitative determination of urinary protein.

1977 ◽  
Vol 23 (5) ◽  
pp. 876-879 ◽  
Author(s):  
W L Gyure
Keyword(s):  
Serum Albumin ◽  
Salt Concentration ◽  
Urine Samples ◽  
Urine Protein ◽  
Sulfosalicylic Acid ◽  
Green Method ◽  
Semiquantitative Determination ◽  
Acid Method ◽  
Bromcresol Green

Abstract Two types of urine protein dipsticks and the sulfosalicylic acid method were compared for their accuracy and specificity, with use of urine samples supplemented with various proteins. Dipsticks yield accurate results when the protein under consideration is restricted to albumin; the sulfosalicylic acid method accurately determines many kinds of proteins in addition to albumin. Detergents affect each of the methods, but changes in salt concentration only affect results by dipstick procedures. Dipsticks, which are based on the protein-error principle for indicators, are subject to some of the conditions that apply to the bromcresol green method for serum albumin determination.

scholarly journals Determination of 1,5‒anhydro‒glucitol–carrier protein conjugates by matrix‒assisted laser desorption/ionization tof mass spectrometry and antibody formation

2000 ◽  
Vol 14 (3) ◽  
pp. 85-92 ◽  
Author(s):  
Li-Jiang Xuan ◽  
Hiroyuki Tanaka ◽  
Satoshi Morimoto ◽  
Yukihiro Shoyama ◽  
Hiroshi Akanuma ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Serum Albumin ◽  
Laser Desorption ◽  
Laser Desorption Ionization ◽  
Protein Conjugates ◽  
Desorption Ionization ◽  
Chicken Lysozyme ◽  
Matrix Assisted Laser ◽  
Matrix Assisted Laser Desorption

In order to prepare the monoclonal antibody against 1,5-anhydro-glucitol (1), it was conjugated with bovine serum albumin (BSA), human serum albumin (HSA) or chicken lysozyme (CL) using succinate orβ-alanine succinate as a spacer to produce individual antigen conjugates. The number of hapten contained in each antigen conjugate was determined by matrix-assisted laser desorption/ionization tof mass (MALDI-tof-MS) spectrometry. The formation of monoclonal antibody (MAb) was also discussed.

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