scholarly journals Tuning the interactions of decavanadate with thaumatin, lysozyme, proteinase K and human serum proteins by its coordination to a pentaaquacobalt(ii) complex cation

2019 ◽  
Vol 43 (45) ◽  
pp. 17863-17871 ◽  
Author(s):  
Lukáš Krivosudský ◽  
Alexander Roller ◽  
Annette Rompel
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Proteins ◽  
Complex Cation ◽  
Proteinase K ◽  
Human Serum Proteins

Inorganic functionalization of the decavanadate anion promotes a different type of interaction with model proteins thaumatin, lysozyme, proteinase K, human serum albumin and transferrin.

Dimeric binding of plant alkaloid ellipticine to human serum proteins

RSC Advances ◽  
2016 ◽  
Vol 6 (50) ◽  
pp. 44096-44105 ◽  
Author(s):  
Ferenc Zsila ◽  
Tamás Beke-Somfai
Keyword(s):  
Circular Dichroism ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Proteins ◽  
Glycoprotein P ◽  
Acid Glycoprotein ◽  
Circular Dichroïsm ◽  
Human Serum Proteins

Induced exciton circular dichroism signals reveal the accommodation of a pair of ellipticine molecules to the subdomain IB of human serum albumin and the β-barrel of α1-acid glycoprotein.

Ausscheidung von 131J-Humanalbumin im Primärharn der Froschniere

1959 ◽  
Vol 14 (5) ◽  
pp. 323-327 ◽  
Author(s):  
Werner Heinzel ◽  
Ekkehard Kallee
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Proteins ◽  
Human Albumin ◽  
Protein Solution ◽  
Bladder Urine

1. The glomerular capsules of 8 Bombinata toads have been tapped. The glomerula have been found to excrete 0.035-0.15 μg of protein in about 0.11 μl of urine per hour, i. e., a 0.1 p.c. protein solution.2. Radioiodinated human serum albumin when injected intraperitoneally was excreted by the toad glomerula into the primary urine and resorbed back by the tubuli in principle in the same ways as toad serum proteins. However, the human albumin was excreted by the glomerula to a significantly larger extent than toad proteins.3. The concentration of both toad protein and 131I-labelled human albumin was approximately seven times lower in the bladder urine than in the primary urine.

Water Proton Relaxation Rate Enhancements and Association Constants for Mn(II) to Serum Proteins Determined by NMR T1 Measurements

2005 ◽  
Vol 60 (9-10) ◽  
pp. 807-812 ◽  
Author(s):  
Hatice Budak
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Relaxation Rate ◽  
Association Constant ◽  
Serum Proteins ◽  
Association Constants ◽  
Water Proton ◽  
Proton Relaxation ◽  
Rate Enhancement ◽  
Human Serum Proteins

Abstract The water proton relaxation rate enhancement of Mn(II) bound to bovine serum albumin (BSA) and the association constant for manganese to BSA have already been determined, but such determinations have not been done for human serum albumin (HSA) and other human serum proteins and also for human serum. In this work, NMR T1 values in aqueous solutions of serum proteins and serum were measured versus increasing concentration of Mn(II). Proton relaxation rate enhancements (ε*) caused by different manganese concentrations were determined for each solution and 1/ε* was fitted against concentrations of Mn(II). Proton relaxation rate enhancements (εb) of Mn(II) bound to albumin, γ-globulin, (α+β)- globulins and serum were found to be 13.69, 3.09, 8.62, and 10.87, respectively. Free and bound manganese fractions, resulted from each addition of Mn(II) to the sample, were determined by using corresponding (ε*) and the εb values. Association constants for Mn(II) to HSA and γ-globulin were calculated as 1.84 x 104 ᴍ-1 and 2.35 x 104 ᴍ-1, respectively. Present data suggest that the proton relaxation rate enhancement of Mn(II) in serum is caused by Mn(II) bound to various serum constituents. Data also suggest that association constants for Mn(II) to γ-globulin are nearly the same as that to HSA.

scholarly journals EVIDENCE FOR SPECIES' DIFFERENCES IN THE EFFECT OF SERUM γ-GLOBULIN CONCENTRATION ON γ-GLOBULIN CATABOLISM

1964 ◽  
Vol 120 (5) ◽  
pp. 967-986 ◽  
Author(s):  
Stewart Sell
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum ◽  
Guinea Pigs ◽  
Serum Proteins ◽  
Elevated Serum ◽  
Keyhole Limpet Hemocyanin ◽  
Normal Numbers ◽  
Γ Globulins

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig γ-globulins and human serum albumin were determined in mice and in guinea pigs whose serum γ-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum γ-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled γ-globulins from all species tested were markedly increased in mice with elevated γ-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit γ-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine γ-globulin were only partially effective, and injections of human serum albumin had no effect. The γ-globulin catabolic rates were decreased in mice with subnormal serum γ-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum γ-globulin levels. In contrast, elevation of the serum γ-globulin levels by injections of exogenous γ-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled γ-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum γ-globulin concentration appears to be operative in the mouse, but not in the guinea pig. Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum γ-globulin levels.

scholarly journals Impact of Human Serum Proteins on Susceptibility of Acinetobacter baumannii to Cefiderocol: role of iron transport

2021 ◽  
Author(s):  
Casin Le ◽  
Camila Pimentel ◽  
Fernando Pasteran ◽  
Marisel Romina Tuttobene ◽  
Tomas Subils ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Human Serum ◽  
Acinetobacter Baumannii ◽  
Iron Uptake ◽  
Iron Transport ◽  
Serum Proteins ◽  
Cell Entry ◽  
Altered Expression ◽  
Human Serum Proteins

Cefiderocol is a siderophore antibiotic that co-opts iron transporters to facilitate cell entry. We show that genes related to iron uptake systems and resistance to β-lactams in Acinetobacter baumannii have altered expression levels in the presence of human serum, human serum albumin, or human pleural fluid. Cefiderocol MICs are also raised in the presence of the mentioned fluids. Clinical response in A. baumannii infections may be related to the interplay of these human factors.

scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

Complexation of Cm(III) with blood serum proteins: recombinant human serum albumin (rHSA)

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Nicole Adam ◽  
Cédric Y. Reitz ◽  
Anna-Lena Ditter ◽  
Petra J. Panak
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Metal Binding ◽  
Serum Proteins ◽  
Laser Fluorescence ◽  
Conditional Stability ◽  
Conditional Stability Constant ◽  
Recombinant Human Serum Albumin

Abstract The complexation of Cm(III) with the recombinant human serum albumin (rHSA) (characterized by single deletion of residue Asp-1), is studied in dependence of pH and rHSA concentration using time-resolved laser fluorescence spectroscopy (TRLFS). A Cm(III) rHSA species is formed between pH 6.4 and 10.0 with the conditional stability constant being logK = 6.47 at pH = 7.4. Competition titration experiments with Cu(II) and Zn(II) confirm complexation at the N-terminal binding site (NTS) of rHSA and exclude the involvement of the Multi-Metal Binding Site (MBS). Comparison with a previous study on Cm(III) interaction with native albumin, HSA, points out, that residue Asp-1 is involved in Cm(III) binding to HSA but is not crucial for Cm(III) complexation at the NTS. The results are of major importance for a better understanding of fundamental actinide-protein interaction mechanisms which are highly required for the identification and characterization of relevant distribution pathways of incorporated radionuclides.

scholarly journals SARS-CoV-2 Spike protein binding of glycated serum albumin - its potential role in the pathogenesis of the COVID-19 clinical syndromes and bias towards individuals with pre-diabetes/type 2 diabetes & metabolic diseases.

2021 ◽  
Author(s):  
Jason K Iles ◽  
Raminta Zmuidinaite ◽  
Christoph Saddee ◽  
Anna Gardiner ◽  
Jonathan Lacy ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Immune Evasion ◽  
Magnetic Beads ◽  
Metabolic Diseases ◽  
Serum Proteins ◽  
Diabetes Type 2 ◽  
Spike Protein ◽  
Albumin Concentration

Since the immune response to SARS-CoV2 infection requires antibody recognition of the Spike protein, we used MagMix, a semi-automated magnetic rack to reproducibly isolate patient plasma proteins bound to a pre-fusion stabilised Spike and nucleocapsid proteins conjugated to magnetic beads. Once eluted, MALDI-ToF mass spectrometry identified a range of immunoglobulins, but also in Spike protein magnetic beads we found a high affinity for human serum albumin. Careful mass comparison revealed a preferential capture of AGE glycated human serum albumin by the pre-fusion Spike protein. The ability of bacteria and viruses to surround themselves with serum proteins is a recognised process of immune evasion. A lower serum albumin concentration is a reported feature of COVID-19 patients with severe symptoms and high probability of death. This binding preference of the Spike protein for AGE glycated serum albumin may contribute to immune evasion and influence the severity & pathology of SARS-COV2 towards acute respiratory distress. Thus contributing to the symptom severity bias and mortality risk for the elderly and those with (pre)diabetic and atherosclerotic/metabolic diseases who contract SARS-CoV2 infections.

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