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Human serum albumin

About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.


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Journal ArticleDOI
TL;DR: The increased formation of serum HNE-modified albumin in type 2 diabetic outpatients in the milieu between liver and vascular lumina, indicating the presence of oxidative stress.
Abstract: 4-Hydroxy-2-nonenal (HNE) is one of the major lipid peroxidation products with cytotoxic and mutagenic activity. It further reacts with protein residues such as histidine to generate stable Michael adducts. To evaluate the status of oxidative stress in the serum of type 2 diabetes mellitus, we constructed a sandwich enzyme-linked immunosorbent assay to measure serum HNE-modified albumin by the use of a specific monoclonal antibody (HNEJ-2) against HNE-histidine adducts as well as an antibody against human serum albumin. Serum of type 2 diabetes outpatients revealed significantly higher levels of HNE-modified albumin (736.1 ± 34.2 pmol/ml, n = 54) than the matched nondiabetics (611.4 ± 39.1 pmol/ml, n = 30; means ± SEM; p = 0.018). However, no significant correlation was observed in diabetic outpatients between the levels of HNE-modified albumin and clinical parameters such as fasted blood glucose, HbA1c, diabetes duration, or complications. Our data demonstrated the increased formation of serum H...

95 citations

Journal ArticleDOI
TL;DR: Time-resolved measurements using laser flash photolysis reveal the presence of two components with different lifetimes in triplet decay, which are ascribed to the CP/HSA complexes in site I, where stereodifferentiation is more important.
Abstract: A remarkable stereodifferentiation has been observed in the interaction between the excited triplet state of carprofen (CP) and human serum albumin (HSA). Time-resolved measurements using laser flash photolysis reveal the presence of two components with different lifetimes in triplet decay. This is explained by complexation of CP to the two possible HSA binding sites. The shorter-lived components are ascribed to the CP/HSA complexes in site I, where stereodifferentiation is more important (tauR/tauS ca. 4). This is correlated with formation of a dehalogenated photoproduct upon steady-state photolysis.

95 citations

Journal ArticleDOI
TL;DR: Both complexes containing the 6-maleimido-4-oxacaproic ester showed good water solubility and CE experiments revealed rapid binding to human serum albumin and the formation of biadducts with dGMP and dAMP.

95 citations

Journal ArticleDOI
TL;DR: Two chelates (N,N′,N″,N‴-pentaacetic acid) bearing different substituents for binding to human serum albumin (HSA) are compared and display an analogous binding affinity for the serum protein.
Abstract: -pentaacetic acid) bearing different substituents for binding to human serum albumin (HSA) are compared. In spite of the structural differences of the recognition synthon and of the residual electric charge, the two chelates display an analogous binding affinity for the serum protein. Upon formation of the adducts with HSA, the exchange rates of the coordinated water appear slowed down by an amount corresponding to ca. 50% of the rates found for the free complexes. The relaxivity of [Gd(BOM)3DTPA (H2O)]2 − is significantly higher than that of MS-325 either in the free complex or in the macromolecular adduct. Finally, the effect of pH on the stability of the HSA adducts and on the values of their relaxivities has been investigated.

95 citations

Journal ArticleDOI
TL;DR: It is speculated that the formation of an M2HsTf complex of high affinity may predict a lobe-closed conformation that leads to a favorable interaction with TfR1, and has implications for the metabolism of Ti(IV) in human serum.
Abstract: The trafficking of titanium(IV) by human serum transferrin (HsTf) has been implicated in the physiology of this hydrolysis-prone metal. The current work broadens to include the further interactions of Ti(IV) in serum that bear on this model. Ti2HsTf (2 equiv) binds the transferrin receptor TfR1 with Kd1 = 6.3 ± 0.4 nM and Kd2 = 410 ± 150 nM, values that are the tightest yet measured for a metal other than iron but weaker than the corresponding ones for Fe2HsTf due to both slightly slower on rates and slightly faster off rates. Comparing the affinities of metals for HsTf with the affinities of the resulting M2HsTf species for TfR1, we speculate that the formation of an M2HsTf complex of high affinity may predict a lobe-closed conformation that leads to a favorable interaction with TfR1. Human serum albumin (HSA), an important serum competitor for metal binding, can bind up to 20 equiv of Ti(IV) supplied in several forms. With some ligands, Ti(IV) may bind to the N-terminal metal binding site of albumin, fo...

95 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023174
2022423
2021284
2020333
2019333
2018337