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.

Neurokinin receptor mediated plasma extravasation in guinea pig and rat airways: comparison of 125I-labelled human fibrinogen and 99mTc-labelIed human serum albumin as markers of leakage

1993 ◽  
Vol 71 (7) ◽  
pp. 506-511 ◽  
Author(s):  
Christine Tousignant ◽  
Chi-Chung Chan ◽  
Donna Young ◽  
Diane Guevremont ◽  
Ian W. Rodger
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum ◽  
Plasma Extravasation ◽  
Human Fibrinogen ◽  
Protein Extravasation ◽  
Neurokinin Receptor ◽  
Lower Airways ◽  
Dose Dependent

In the present study we have characterized NK-1 and NK-2 receptor induced microvascular leakage in guinea pig and rat airways, using 125I-labelled human fibrinogen ([125I]FN) versus 99mTc-labelled human serum albumin ([99mTc]HSA) as markers for plasma protein extravasation. Intravenous administration of the selective NK-1 agonist [Sar9, Met(O2)11]SP (1 nmol kg−1) caused a dose-dependent increase of [125I]FN extravasation in guinea pig trachea, main bronchi, secondary bronchi, and intraparenchymal airways. Extravasation of [125I]FN increased by up to 192 (trachea), 284 (main bronchi), 368 (secondary bronchi), and 271% (intraparenchymal bronchi) over control levels in these regions of the airways. Pretreatment of the animals with CP 99,994 and RP 67,580, two NK-1 nonpeptide antagonists, caused a dose-dependent inhibition of [Sar9, Met(O2)11]SP-induced leakage of [125I]FN. [Sar9, Met(O2)11]SP (1 nmol kg−1) did not induce specific leakage of [99mTc]HSA in the intraparenchymal bronchi. Specific NK-2 receptor induced leakage was detected in the lower airways but only when using [125I]FN as a marker. We have also compared the ability of CP 99,994 and RP 67,580 to inhibit [Sar9, Met(O2)11]SP induced extravasation of [125I]FN in rat airways. CP 99,994 was 40–50 (tracheobronchial region) to 75 (lower airways) times more potent in the guinea pig than the rat airways. In contrast, RP 67,580 had higher affinity for rat airways compared with guinea pig airways. The results of this study highlight the superiority of [125I]FN as a sensitive marker of plasma extravasation over [99mTc]HSA. Furthermore, the results strongly suggest that both NK-1 and NK-2 receptors mediate plasma extravasation in the guinea pig lower airways and that NK-1 receptors are different in guinea pig and rat airways.Key words: Leakage, tachykinins, NK-1 and NK-2 receptors, airway, asthma.

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.

Further Studies on Guinea Pig and Rabbit Cytophilic Antibodies Directed Against Human Serum Albumin

1972 ◽  
Vol 42 (3) ◽  
pp. 399-429 ◽  
Author(s):  
P.C. Maginn ◽  
L. Sparr ◽  
K. Daniel ◽  
A.A. Blazkovec
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum

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.

Thermodynamics of the Interaction Between Graphene Quantum Dots with Human Serum Albumin and γ-Globulins

2020 ◽  
Vol 49 (1) ◽  
pp. 100-116 ◽  
Author(s):  
Xiao-Xu Ba ◽  
Tian Gao ◽  
Mian Yang ◽  
Peng Jiang ◽  
Feng-Lei Jiang ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Graphene Quantum Dots ◽  
Γ Globulins

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.

Interactions between carbon nanodots with human serum albumin and γ-globulins: The effects on the transportation function

2016 ◽  
Vol 301 ◽  
pp. 242-249 ◽  
Author(s):  
Zi-Qiang Xu ◽  
Qi-Qi Yang ◽  
Jia-Yi Lan ◽  
Jia-Qi Zhang ◽  
Wu Peng ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carbon Nanodots ◽  
Γ Globulins

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.

THE EFFECT OF FREE FATTY ACIDS ON RESIN UPTAKE OF TRI-IODOTHYRONINE FROM HUMAN, RAT, RABBIT AND GUINEA-PIG SERUM AND HUMAN SERUM ALBUMIN

1969 ◽  
Vol 45 (4) ◽  
pp. 489-493 ◽  
Author(s):  
P. W. NATHANIELSZ
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Free Fatty Acids ◽  
Human Serum ◽  
Rat Serum ◽  
Pig Serum

SUMMARY Recently changes in plasma free fatty acids have been suggested as a possible regulator of the levels of free thyroxine in the plasma. Oleic acid has been shown to displace tri-iodothyronine from human serum, human serum albumin, rat serum, rabbit serum and guinea-pig serum. The extent of the displacement, much greater from human serum albumin than from whole serum, suggests that free fatty acid does not affect the globulin binding site. It would also appear that, in the rat, all the binding sites are sensitive to free fatty acids and hence there is probably only albumin binding in this species. The results with rabbit and guinea-pig serum were intermediate to those with human and rat serum. A significant rise in resin uptake of tri-iodothyronine in vitro occurred with an increase of free fatty acid level of 0·5 m-equiv./l., well within the physiological range.

Sign in / Sign up

Export Citation Format

Share Document