scholarly journals Human Serum Albumin Cys34Oxidative Modifications following Infiltration in the Carotid Atherosclerotic Plaque

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Antonio Junior Lepedda ◽  
Angelo Zinellu ◽  
Gabriele Nieddu ◽  
Pierina De Muro ◽  
Ciriaco Carru ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carotid Endarterectomy ◽  
Atherosclerotic Plaque ◽  
Plasma Samples ◽  
Carotid Atherosclerotic Plaque ◽  
Sds Page ◽  
Oxidative Modifications ◽  
First Time

Objectives.To evaluate if the prooxidant environment present in atherosclerotic plaque may oxidatively modify filtered albumin.Methods.Fluorescein-5-maleimide labelled plasma samples and plaque extracts from 27 patients who had undergone carotid endarterectomy were analysed through nonreducing SDS-PAGE for albumin-Cys34oxidation. Furthermore, degree and pattern of S-thiolation in both circulating and plaque-filtered albumin were assayed.Results.Albumin filtered in the atherosclerotic plaque showed higher levels of Cys34oxidative modifications than the corresponding circulating form as well as different patterns of S-thiolation.Conclusions.Data indicate that the circulating albumin, once filtered in plaque, undergoes Cys34oxidative modifications and demonstrate for the first time that albumin is a homocysteine and cysteinylglycine vehicle inside the plaque environment.

scholarly journals First Immunoassay for Measuring Isoaspartate in Human Serum Albumin

Molecules ◽  
2021 ◽  
Vol 26 (21) ◽  
pp. 6709
Author(s):  
Jijing Wang ◽  
Susanna L. Lundström ◽  
Sven Seelow ◽  
Sergey Rodin ◽  
Zhaowei Meng ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Plasma Samples ◽  
Donor Blood ◽  
Average Value ◽  
First Time

Isoaspartate (isoAsp) is a damaging amino acid residue formed in proteins mostly as a result of spontaneous deamidation of asparaginyl residues. An association has been found between isoAsp in human serum albumin (HSA) and Alzheimer’s disease (AD). Here we report on a novel monoclonal antibody (mAb) 1A3 with excellent specificity to isoAsp in the functionally important domain of HSA. Based on 1A3 mAb, an indirect enzyme-linked immunosorbent assay (ELISA) was developed, and the isoAsp occupancy in 100 healthy plasma samples was quantified for the first time, providing the average value of (0.74 ± 0.13)%. These results suggest potential of isoAsp measurements for supplementary AD diagnostics as well as for assessing the freshness of stored donor blood and its suitability for transfusion.

Strategy for identification and detection of multiple oxidative modifications within proteins applied on persulfate-oxidized hemoglobin and human serum albumin

2010 ◽  
Vol 25 (2) ◽  
pp. 327-340 ◽  
Author(s):  
Harriet Mörtstedt ◽  
Marina C. Jeppsson ◽  
Giovanni Ferrari ◽  
Bo A.G. Jönsson ◽  
Monica H. Kåredal ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Oxidative Modifications

Spectroscopic and molecular modeling studies of human serum albumin interaction with propyl gallate

RSC Advances ◽  
2014 ◽  
Vol 4 (110) ◽  
pp. 64559-64564 ◽  
Author(s):  
Jafar Ezzati Nazhad Dolatabadi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Ali Akbar Jamali ◽  
Fahimeh Kheirdoosh ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Propyl Gallate ◽  
Fluorescence Quenching Method ◽  
Molecular Modeling Studies ◽  
Quenching Method ◽  
First Time

For the first time, PG interaction with HSA using fluorescence quenching method, circular dichroism spectroscopy and molecular modeling was investigated.

Cisplatin binding to human serum albumin: a structural study

2015 ◽  
Vol 51 (46) ◽  
pp. 9436-9439 ◽  
Author(s):  
Giarita Ferraro ◽  
Lara Massai ◽  
Luigi Messori ◽  
Antonello Merlino
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Crystal Structures ◽  
Structural Study ◽  
X Ray ◽  
X Ray Crystallography ◽  
First Time

The reaction between cisplatin and human serum albumin (HSA) was investigated by X-ray crystallography and crystal structures of the cisplatin/HSA adduct were eventually solved for the first time.

Effect of Severe Hypoxia on Blood-Cerebrospinal Fluid Barrier

1957 ◽  
Vol 190 (2) ◽  
pp. 365-370 ◽  
Author(s):  
Lawrence B. Slobody ◽  
Dorothy C. Yang ◽  
Miriam Lending ◽  
Frank J. Borrelli ◽  
Marjorie Tyree
Keyword(s):  
Cerebrospinal Fluid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Concentration Ratio ◽  
Pressure Chamber ◽  
Severe Hypoxia ◽  
Plasma Samples ◽  
Intratracheal Administration ◽  
And Control

The effect of severe hypoxia on the blood-cerebrospinal fluid barrier of dogs was evaluated from the rate of passage of radioiodinated human serum albumin from plasma to cisternal fluid. Hypoxia was induced by intratracheal administration of varying mixtures of O2 and N2 or by use of a Smith-Jones pressure chamber. Radioiodinated albumin was injected intravenously and cisternal fluid and plasma samples were obtained at various intervals thereafter in experimental and control animals. Hypoxia maintained for 1 hour or longer resulted in a marked increase in the concentration ratio (cisternal fluid radioactivity)/(plasma radioactivity). The concentration ratio was frequently higher after 4 hours of hypoxia than after 24–48 hours in control animals. The slope of CSF albumin-I131 concentration as a function of time for the hypoxic animals was about five times that for the control animals. It is concluded that changes in rate of passage of albumin from plasma into cisternal fluid reflect alterations in the permeability of the blood-cerebrospinal fluid barrier to albumin.

scholarly journals Magnetic Immobilization of Pichia pastoris Cells for the Production of Recombinant Human Serum Albumin

Nanomaterials ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 111 ◽  
Author(s):  
Seyedeh-Masoumeh Taghizadeh ◽  
Alireza Ebrahiminezhad ◽  
Mohammad Bagher Ghoshoon ◽  
Ali Dehshahri ◽  
Aydin Berenjian ◽  
...  
Keyword(s):  
Magnetic Field ◽  
Human Serum Albumin ◽  
Pichia Pastoris ◽  
Serum Albumin ◽  
Human Serum ◽  
Novel Approach ◽  
Nanoparticles Concentration ◽  
Complete Cell ◽  
First Time ◽  
Magnetic Immobilization

Magnetic immobilization as a novel technique was used to immobilize recombinant Pichia pastoris (GS115 Albumin) cells to produce human serum albumin (HSA). In this regard, magnetic nanoparticles (MNPs) coated with amino propyl triethoxy silane (APTES) were synthesized. P. pastoris cells were decorated with MNPs via nonspecific interactions. Decorated cells were magneto-responsible and easily harvested by applying an external magnetic field. The efficiency of magnetic immobilization (Ei) for cell removal was in direct relation with the MNP concentration and time of exposure to the magnetic field. By increasing the nanoparticles concentration, cells were harvested in a shorter period. Complete cell removal (Ei ≈ 100) was achieved in ≥0.5 mg/mL of MNPs in just 30 s. HSA is produced in an extremely high cell density (OD ~20) and it is the first time that magnetic immobilization was successfully employed for harvesting such a thick cell suspension. After 5 days of induction the cells, which were immobilized with 0.25 to 1 mg/mL of nanoparticles, showed an increased potency for recombinant HSA production. The largest increase in HSA production (38.1%) was achieved in the cells that were immobilized with 0.5 mg/mL of nanoparticles. These results can be considered as a novel approach for further developments in the P. pastoris-based system.

Enantioseparation, recognition mechanisms and binding of xanthones on human serum albumin by liquid chromatography

Bioanalysis ◽  
2019 ◽  
Vol 11 (13) ◽  
pp. 1255-1274 ◽  
Author(s):  
João P do Carmo ◽  
Ye Zaw Phyo ◽  
Andreia Palmeira ◽  
Maria Elizabeth Tiritan ◽  
Carlos Afonso ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Mobile Phase ◽  
Chiral Recognition ◽  
Chiral Stationary Phase ◽  
Organic Modifier ◽  
First Time ◽  
Derivatives Of

Aim: To develop a method for enantioseparation of several chiral derivatives of xanthones (CDXs) by LC using a human serum albumin-chiral stationary phase (HSA-CSP) and screening CDX-HSA affinity. Additionally, recognition mechanisms were investigated. Materials & methods: The influence of organic modifier, buffer type, pH and ionic strength of mobile phase, and temperature were explored. The affinity was determined by measuring the retention times and further calculation of bound percentage. Chiral recognition mechanisms were investigated by docking. Results: Enantioselectivity and resolution values ranged from 1.40 to 9.16 and 1.51 to 4.97. Bound percentages ranged from 79.02 to 99.99%. Conclusion: LC systematic study and binding affinity of CDXs on HSA-CSP are presented here for the first time, expanding the applications of HSA-CSP for this class of compounds.

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