Preparation and Properties of Serum and Plasma Proteins. XXXI. An Optical and Morphological Study of Some Crystalline Human Serum Albumin Preparations and of Their Derivatives1a,1b

1951 ◽  
Vol 73 (8) ◽  
pp. 3911-3916 ◽  
Author(s):  
Barbara W. Low ◽  
E. J. Weichel
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Plasma Proteins ◽  
Morphological Study

Influence of Human Serum Albumin Glycation on the Binding Affinities for Natural Flavonoids

2019 ◽  
Vol 17 (1) ◽  
pp. 806-812
Author(s):  
Liangliang Liu ◽  
Yi Liu ◽  
Aiping Xiao ◽  
Shiyong Mei ◽  
Yixi Xie
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Small Molecules ◽  
Human Body ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fluorescence Spectra ◽  
Binding Affinities ◽  
Dietary Flavonoids

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.

Binding of Testosterone and Oestradiol to Sex Hormone Binding Globulin, Human Serum Albumin and other Plasma Proteins: Evidence for Non-Specific Binding of Oestradiol to Sex Hormone Binding Globulin

1983 ◽  
Vol 64 (3) ◽  
pp. 307-314 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Maureen Dalton ◽  
Robert S. Sawers
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Plasma Proteins ◽  
Specific Binding ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Normal Female ◽  
Hormone Binding

1. The percentage binding of testosterone (T) and oestradiol (E2) to sex hormone binding globulin (SHBG) and human serum albumin (HSA) was determined over a range of SHBG concentrations of 16–250 nmol of dihydrotestosterone (DHT) bound/l. It was found that the binding of both T and E2 to HSA was a function of their binding to SHBG and bore an inverse relationship to it. After removal of both SHBG and HSA from plasma by affinity chromatography a ‘residual’ binding of about 11% for T and 12% for E2 was still apparent. in addition to the specific high-affinity, low capacity binding of E2 to SHBG, non-specific low-affinity binding of 7–12% was demonstrated after selective denaturation of the specific binding site of the latter. 2. Competition studies indicated that although at the relatively higher levels of SHBG found in the normal female the physiological concentrations of E2, T and DHT need not be taken into account in estimating the unbound fractions of steroids, at the relatively lower levels of SHBG found in normal men and hirsute women, the physiological concentrations of T and DHT are effective in causing statistically significant displacement of E2 from the common, specific binding site on SHBG. 3. A simple computerized technique is described for the determination of fractions of E2 and T respectively, that are unbound to SHBG, unbound to SHBG and HSA, and unbound to all plasma proteins, when the total plasma levels of E2, T, DHT and SHBG are known.

A novel 3D-printed centrifugal ultrafiltration method reveals in vivo glycation of human serum albumin decreases its binding affinity for zinc

Metallomics ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 1036-1043 ◽  
Author(s):  
Monica J. Jacobs ◽  
Cody W. Pinger ◽  
Andre D. Castiaux ◽  
Konnor J. Maloney ◽  
Dana M. Spence
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Glucose ◽  
Plasma Proteins ◽  
Structure And Function ◽  
3D Printed ◽  
And Function ◽  
Centrifugal Ultrafiltration

Plasma proteins are covalently modified in vivo by the high-glucose conditions in the bloodstreams of people with diabetes, resulting in changes to both structure and function.

Electrokinetic chromatographic estimation of the enantioselective binding of nomifensine to human serum albumin and total plasma proteins

2012 ◽  
Vol 26 (11) ◽  
pp. 1357-1363 ◽  
Author(s):  
Lucía Asensi-Bernardi ◽  
Yolanda Martín-Biosca ◽  
Salvador Sagrado ◽  
María J. Medina-Hernández
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Plasma Proteins ◽  
Total Plasma

scholarly journals Influence of core and maltose surface modification of PEIs on their interaction with plasma proteins—Human serum albumin and lysozyme

2017 ◽  
Vol 152 ◽  
pp. 18-28 ◽  
Author(s):  
Dominika Wrobel ◽  
Monika Marcinkowska ◽  
Anna Janaszewska ◽  
Dietmar Appelhans ◽  
Brigitte Voit ◽  
...  
Keyword(s):  
Surface Modification ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Plasma Proteins

scholarly journals Relationship of large hepatitis B surface antigen polypeptide to human serum albumin

1980 ◽  
Vol 28 (2) ◽  
pp. 459-463
Author(s):  
J W Shih ◽  
P L Tan ◽  
J L Gerin
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Hepatitis B ◽  
Serum Albumin ◽  
Human Serum ◽  
Surface Antigen ◽  
Plasma Proteins ◽  
Hepatitis B Surface Antigen ◽  
Significant Proportion ◽  
Relationship Of

A significant proportion (20 to 40%) of highly purified 22-nm hepatitis B surface antigen (HBsAg) particles contain human serum albumin (HSA) as demonstrated by specific precipitation of radioiodinated particles by anti-HSA. Preparations of the isolated major HBsAg polypeptides (P-1, P-2, and P-6) were iodinated and analyzed by radiommunoprecipitation for reactivity with rabbit antisera to human plasma proteins. Only the P-6 fraction (molecular weight, 68,000) was precipitated and only by anti-HSA; specific precipitation was observed with guinea pig antisera to P-6 and native HBsAg and goat or rabbit antisera to HSA. Coprecipitation of P-6 with antiserum to HBsAg and with anti-HSA, compared to precipitation with each antiserum alone, indicated that the HBsAg and HSA determinants were on separate molecules. The P-6 polypeptide may represent a precursor protein of the hepatitis B virion.

Computational prediction of interaction and pharmacokinetics profile study for polyamino-polycarboxylic ligands on binding with human serum albumin

2020 ◽  
Vol 44 (7) ◽  
pp. 2907-2918 ◽  
Author(s):  
Nidhi Chadha ◽  
Dushyant Singh ◽  
Marilyn D. Milton ◽  
Gauri Mishra ◽  
Joseph Daniel ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Computational Prediction ◽  
Profile Study ◽  
Drugs And Metabolites

Human serum albumin (HSA) is one of the most abundant plasma proteins available in blood and responsible for transport of fatty acids, drugs and metabolites at its binding sites which are very important for the assessment of pharmacokinetics profile of the polyamino-polycarboxylic ligands.

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