Covalent Binding of the Flavonoid Quercetin to Human Serum Albumin

2005 ◽  
Vol 53 (10) ◽  
pp. 4194-4197 ◽  
Author(s):  
Mark I. Kaldas ◽  
U. Kristina Walle ◽  
Hester van der Woude ◽  
JoEllyn M. McMillan ◽  
Thomas Walle
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Covalent Binding ◽  
Flavonoid Quercetin

RADIOIMMUNOASSAYS OF 3,5,3′-TRIIODO-L-THYRONINE WITH AND WITHOUT A PRIOR EXTRACTION STEP

1975 ◽  
Vol 80 (1) ◽  
pp. 58-69 ◽  
Author(s):  
A. Burger ◽  
C. Sakoloff ◽  
V. Staeheli ◽  
M. B. Vallotton ◽  
S. H. Ingbar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Normal Values ◽  
Covalent Binding ◽  
Extraction Procedure ◽  
Mixed Population ◽  
Coupling Agents ◽  
Extraction Step ◽  
The Mean

ABSTRACT Two radioimmunoassays for triiodothyronine (T3) are described, one of which includes an extraction step, while the other does not. To raise antibodies, two carrier proteins and different coupling agents were used, namely haemocyanin and diazotized benzidine or human serum albumin and carbodiimide. In the case of T3 coupled to haemocyanin by diazotized benzidine, evidence of covalent binding of the hapten to the protein was obtained. In the case of T3 coupled to human serum albumin, little evidence of covalent linkage was available. Nevertheless immunization was successful in both cases. The radioimmunoassay in unextracted serum was highly reproducible and precise (intra-assay variability 5.2% inter-assay variability 8.1%). Normal values were determined which clearly indicate a fall in the serum T3 concentration with increasing age. In men the fall occurs in the fifth decade. In women the T3 starts to fall only after 70 years of age. In 31 cases of hyperthyroidism the serum T3 concentration ranged from 2.26 to 10.4 ng T3/ml. In 10 cases of hypothyroidism the values ranged from 0 to 0.8 ng T3/ml. The radioimmunoassay using an extraction procedure was less extensively used since it was found to be less reproducible (intra-assay variability 7.5%, inter-assay 12.25%). The normal values were determined with a mixed population aged 20–50. The mean ± 2 sd was 0.9 ± 0.36 ng T3/ml (n=52). In 17 cases of hypothyroidism the values ranged from 0 to 0.6 ng T3/ml and in 22 cases of hyperthyroidism from 2 to 14.4 ng T3/ml.

scholarly journals Analysis of Binding Interactions of Ramipril and Quercetin on Human Serum Albumin: A Novel Method in Affinity Evaluation

Molecules ◽  
2020 ◽  
Vol 25 (3) ◽  
pp. 547
Author(s):  
Zuzana Vaneková ◽  
Lukáš Hubčík ◽  
José Luis Toca-Herrera ◽  
Paul Georg Furtműller ◽  
Pavel Mučaji ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Accurate Method ◽  
Cd Spectroscopy ◽  
Future Research ◽  
Binding Interactions ◽  
Allosteric Interactions ◽  
Flavonoid Quercetin ◽  
High Concentrations

The aim of this study was to analyze the binding interactions between a common antihypertensive drug (ramipril, R) and the widely distributed plant flavonoid quercetin (Q), in the presence of human serum albumin (HSA). From the observed fluorescence spectra of the (HSA + R) system we can assume that ramipril is also one of the Site 3 ligands—similar to fusidic acid—the binding of which has been proven by RTG crystallography. Our claim is supported by near-UV CD spectroscopy, microscale themophoresis and molecular modeling. The presence of R slightly inhibited the subsequent binding of Q to HSA and, on the contrary, the pre-incubation of HSA with Q caused a stronger binding of R, most likely due to allosteric interactions. At high concentrations, R is also able to displace Q from its binding site. The dissociation constant KD for the binding of R is more than hundredfold larger than for Q, which means that R is a very weak binder to HSA. The knowledge of qualitative and quantitative parameters of R, as well as the methods used in this study, are important for future research into HSA binding. This study shows the importance of implementing other methods for KD determination. Microscale thermophoresis has proved to be a novel, practical and accurate method for KD determination on HSA, especially in cases when fluorescence spectroscopy is unable to produce usable results.

Kinetic Analysis of the Covalent Binding of Captopril to Human Serum Albumin

1997 ◽  
Vol 86 (2) ◽  
pp. 215-219 ◽  
Author(s):  
Ryuichi Narazaki ◽  
Kumiko Harada ◽  
Atsushi Sugii ◽  
Masaki Otagiri
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinetic Analysis ◽  
Covalent Binding

scholarly journals Covalent binding of cefotaxime to human serum albumin.

1983 ◽  
Vol 6 (2) ◽  
pp. 139-140 ◽  
Author(s):  
TOSHIMASA TOYO'OKA ◽  
AKIMITSU SANO ◽  
TAKEO KURIKI ◽  
NOBUO SUZUKI
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Covalent Binding

Reversible Covalent Binding of Neratinib to Human Serum Albumin In Vitro

2010 ◽  
Vol 4 (4) ◽  
pp. 220-227 ◽  
Author(s):  
Appavu Chandrasekaran ◽  
Li Shen ◽  
Susan Lockhead ◽  
Aram Oganesian ◽  
Jianyao Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Covalent Binding ◽  
Reversible Covalent

scholarly journals Photoactivated covalent binding of [3H]bilirubin to human serum albumin

1979 ◽  
Vol 181 (3) ◽  
pp. 779-781 ◽  
Author(s):  
D W Hutchinson ◽  
D S Mutopo
Keyword(s):  
Aqueous Solution ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Good Yield ◽  
Covalent Binding ◽  
Covalent Attachment ◽  
Step Procedure ◽  
One Step ◽  
Degradation Studies

A one-step procedure has been developed for the preparation of [3H]bilirubin IX-alpha in good yield from unlabelled bilirubin. Irradiation of an aqueous solution of [3H]bilirubin IX-alpha in the presence of human serum albumin results in the covalent attachment of the bilirubin to the protein. Preliminary degradation studies have been carried out to locate the site of attachment of the bilirubin to the albumin.

Sign in / Sign up

Export Citation Format

Share Document