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 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 Separation of antigens by immunological specificity. Studies on the desorption of homologous antigen from disulphide-linked antibody immunosorbents

1970 ◽  
Vol 117 (1) ◽  
pp. 49-55 ◽  
Author(s):  
J. W. Chidlow ◽  
J. Stephen ◽  
H. Smith
Keyword(s):  
Hydrochloric Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cellulose Acetate ◽  
Cellulose Acetate Electrophoresis ◽  
Acid Buffer ◽  
Homologous Antigen ◽  
Immunological Specificity

1. Glycine–hydrochloric acid buffer, pH2.2, desorbed 131I-labelled human serum albumin (100%), lysozyme (100%), ovalbumin (90%), fluorescent ovalbumin (50–60%) and fluorescent human γ-globulin (20%) from their respective homologous disulphide-linked antibody immunosorbents; reasons are suggested for the low recoveries of the fluorescently labelled proteins. 2. Approx. 40% of the recovered 131I-labelled human serum albumin and fluorescent ovalbumin was desorbed above pH6.0, but lysozyme was not eluted until the pH was 3.0 or below. 3. In all cases where high recoveries of antigen were obtained, the immunosorbents could be regenerated and recycled at least four times with full retention of specificity and minimal diminution of capacity. 4. The desorbed antigens were unchanged when compared with the original antigens by quantitative precipitin, specificradioactivity, fluorescent and enzymic analyses and by cellulose acetate electrophoresis. 5. Desorption of antigen with a variety of reagents was investigated. These reagents were less satisfactory than glycine–hydrochloric acid.

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

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%.

A high-capacity hydrophobic adsorbent for human serum albumin

1985 ◽  
Vol 151 (2) ◽  
pp. 438-441 ◽  
Author(s):  
Makonnen Belew ◽  
Elbert A. Peterson ◽  
Jerker Porath
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Capacity

scholarly journals The specificity of antisera against crystalline serum albumin

1939 ◽  
Vol 39 (2) ◽  
pp. 170-180 ◽  
Author(s):  
Muriel E. Adair ◽  
John Hamilton
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Horse Serum ◽  
Optimal Point ◽  
Homologous Antigen ◽  
Antigen Antibody

Antisera prepared in the rabbit by injection of crystalline horse-serum albumin or crystalline human-serum albumin show a considerable diminution in specificity after more than one course of six to eight injections has been given.The ratio of precipitate nitrogen to antigen nitrogen at the optimal point is smaller in antisera obtained after one course of injections than in antisera derived from subsequent bleedings.In the case of antisera obtained from first bleedings, the ratio of precipitate nitrogen to antigen nitrogen determined at the optimal point with homologous antigen is of approximately the same value in both the antigen-antibody systems studied. The increase in the values of the ratios for antisera from subsequent bleedings is also the same for both systems.

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