High Efficiency Photolabeling of Human Serum Albumin and Human .gamma.-Globulin with [14C]Methyl 4-Azido-2,3,5,6-tetrafluorobenzoate

1995 ◽  
Vol 6 (5) ◽  
pp. 630-634 ◽  
Author(s):  
Raghoottama S. Pandurangi ◽  
Srinivasa R. Karra ◽  
Robert R. Kuntz ◽  
Wynn A. Volkert
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Efficiency ◽  
Gamma Globulin ◽  
Human Gamma Globulin

Changes in Protein Adsorption on Self-Assembled Monolayers with Monolayer Order:  Comparison of Human Serum Albumin and Human Gamma Globulin

Langmuir ◽  
2001 ◽  
Vol 17 (24) ◽  
pp. 7645-7651 ◽  
Author(s):  
Stanislaw Petrash ◽  
Tricia Cregger ◽  
Bin Zhao ◽  
Elena Pokidysheva ◽  
Mark D. Foster ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Adsorption ◽  
Gamma Globulin ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Human Gamma Globulin ◽  
Order Comparison

scholarly journals Separation of antigens by immunological specificity. Use of cellulose-linked antibodies as immunosorbents

1966 ◽  
Vol 101 (3) ◽  
pp. 711-716 ◽  
Author(s):  
RGC Gallop ◽  
BT Tozer ◽  
J Stephen ◽  
H Smith
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gamma Globulin ◽  
High Specificity ◽  
Immunological Specificity

1. Immunosorbents were prepared by coupling activated aminocellulose with the gamma-globulin concentrates of antisera prepared against ovalbumin and human serum albumin. 2. The immunosorbents were low in solubility, but high in capacity for homologous antigens. 3. The high specificity of these immunosorbents was demonstrated by their use in fractionating various mixtures of fluorescent ovalbumin, (131)I-labelled human serum albumin, lysozyme and ribonuclease.

scholarly journals High-efficiency production of human serum albumin in the posterior silk glands of transgenic silkworms, Bombyx mori L

PLoS ONE ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. e0191507 ◽  
Author(s):  
Qiujie Qian ◽  
Zhengying You ◽  
Lupeng Ye ◽  
Jiaqian Che ◽  
Yiran Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bombyx Mori ◽  
High Efficiency ◽  
Silk Glands ◽  
Transgenic Silkworms ◽  
Bombyx Mori L

scholarly journals Separation of antigens by immunological specificity. Use of disulphide-linked antibodies as immunosorbents

1966 ◽  
Vol 101 (3) ◽  
pp. 717-720 ◽  
Author(s):  
J Stephen ◽  
RGC Gallop ◽  
H Smith
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gamma Globulin ◽  
High Capacity ◽  
High Specificity ◽  
Homologous Antigen ◽  
Immunological Specificity ◽  
Insoluble Polymers ◽  
Low Solubility

1. gamma-Globulin concentrates of antisera prepared against ovalbumin and human serum albumin were thiolated and cross-linked to form insoluble polymers. 2. These immunosorbents were of low solubility and of high capacity for homologous antigen. 3. The high specificity of these immunosorbents was demonstrated by fractionation of various binary mixtures of fluorescent ovalbumin, (131)I-labelled human serum albumin, lysozyme and ribonuclease.

scholarly journals Chemical and Physical Characterisation of Macroaggregated Human Serum Albumin: Strength and Specificity of Bonds with 99mTc and 68Ga

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 404
Author(s):  
Letizia Canziani ◽  
Manuela Marenco ◽  
Giorgio Cavenaghi ◽  
Giulia Manfrinato ◽  
Angelo Taglietti ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Efficiency ◽  
Physical Chemical ◽  
Size Dimension ◽  
Commercial Kits ◽  
The Stability ◽  
Optimal Ph

Background: Macroaggregated human serum albumin (MAA) properties are widely used in nuclear medicine, labelled with 99mTc. The aim of this study is to improve the knowledge about the morphology, size, dimension and physical–chemical characteristics of MAA and their bond with 99mTc and 68Ga. Methods: Commercial kits of MAA (Pulmocis®) were used. Characterisation through experiments based on SEM, DLS and Stokes’ Law were carried out. In vitro experiments for Langmuir isotherms and pH studies on radiolabelling were performed and the stability of the radiometal complex was verified through competition reactions. Results: The study settles the MAA dimension within the range 43–51 μm. The Langmuir isotherm reveals for [99mTc]MAA: Bmax (46.32), h (2.36); for [68Ga]MAA: Bmax (44.54), h (0.893). Dual labelling reveals that MAA does not discriminate different radioisotopes. Experiments on pH placed the optimal pH for labelling with 99mTc at 6. Conclusion: Radiolabelling of MAA is possible with high efficiency. The nondiscriminatory MAA bonds make this drug suitable for radiolabelling with different radioisotopes or for dual labelling. This finding illustrates the need to continue investigating MAA chemical and physical characteristics to allow for secure labelling with different isotopes.

THE METABOLISM OF ANTIGENS IN VIVO: I. PROTEIN ANTIGENS

1964 ◽  
Vol 42 (6) ◽  
pp. 821-832
Author(s):  
M. Richter ◽  
C. Larose ◽  
B. Rose
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Gamma Globulin ◽  
Double Diffusion ◽  
Protein Antigens ◽  
Single Intravenous Injection ◽  
Human Gamma Globulin ◽  
Antigen Interaction

Attempts were made to detect antigenic fragments in the sera or spleens of rabbits given a single intravenous injection of bovine serum albumin, human gamma-globulin, or human serum albumin. The results obtained, using a number of different methods for the detection of antibody–antigen interaction (double diffusion in gel, immunoelectrophoresis, inhibition of hemagglutination), failed to provide any evidence in favor of the presence of antigenic fragments either in the circulation or in the spleen of the experimental animal.

scholarly journals An Escherichia coli trap in human serum albumin microtubes

2014 ◽  
Vol 50 (68) ◽  
pp. 9640-9643 ◽  
Author(s):  
S. Yuge ◽  
M. Akiyama ◽  
T. Komatsu
Keyword(s):  
Magnetic Field ◽  
Escherichia Coli ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Efficiency ◽  
Pore Space ◽  
One Dimensional ◽  
E Coli

Human serum albumin microtubes captured Escherichia coli (E. coli) into their one-dimensional pore space interior with a high efficiency. Similar MTs including an Fe3O4 layer also captured E. coli and were manipulated by a magnetic field.

Synthesis of conjugates of 5'-O-carboxymethyl-5-halogeno-2'-deoxyuridines and 5'-O-carboxymethyl-5-halogenouridines with proteins

1980 ◽  
Vol 45 (2) ◽  
pp. 606-610 ◽  
Author(s):  
Helmut Pischel ◽  
Antonín Holý ◽  
Günther Wagner
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gamma Globulin ◽  
Isobutyl Chloroformate ◽  
Mixed Anhydrides ◽  
Covalently Bound

5'-O-Carboxymethyl-2'-deoxyuridine (Ia), its 5-fluoro, 5-bromo and 5-iodo derivatives Ib-Id, and 5'-O-carboxymethyluridine (IIa) and its 5-halogeno derivatives IIb-IId, on reaction with isobutyl chloroformate and tri-n-butylamine afforded mixed anhydrides IIIa-IIId and IVa-IVd. Condensation of III and IV with human serum albumin or bovine gamma-globulin at pH 8.0 gave conjugates Va-Vd to VIIIa-VIIId, the yield of the covalently bound haptene being 28 to 43%.

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