Results 171 to 180 of about 24,729 (207)
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Binding of rabbit immunoglobulin G Fab fragments to subtilisin Carlsberg
Molecular Immunology, 1973Abstract The interaction of crystalline subtilisn Carlsberg with pooled rabbit anti-subtilisin serum was studied by classical precipitin reaction techniques. In addition, Fab fragments were obtained from the rabbit immunoglobulins precipitated by subtilisin, and the interaction between Fab fragments and antigen was studied in the analytical ...
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Disposition of a monoclonal anti-phencyclidine Fab fragment of immunoglobulin G in rats.
The Journal of Pharmacology and Experimental Therapeutics, 1993Treatment of drug toxicity is problematic for compounds like phencyclidine (PCP) which have no known antagonists. With the advent of technology for production of large amounts of monoclonal antibody, it is now possible to explore the use of these antibodies as high affinity in vivo antagonists for treatment of PCP overdose.
M B, McClurkan +3 more
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International Journal of Biological Macromolecules, 2021
The antigen binding fragment (Fab) is pepsin-digested product from egg yolk immunoglobulin (IgY), which shows lower immunogenicity and higher antibacterial activity. However, it limited the application of Fab due to the spontaneous adsorption and aggregation at the air-liquid interface.
Zhaoxia Cai +4 more
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The antigen binding fragment (Fab) is pepsin-digested product from egg yolk immunoglobulin (IgY), which shows lower immunogenicity and higher antibacterial activity. However, it limited the application of Fab due to the spontaneous adsorption and aggregation at the air-liquid interface.
Zhaoxia Cai +4 more
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Human Antibodies, 1994
We have developed PCR primers for the amplification and cloning of the genes encoding human antibody fragments. Two sets of primers were designed to amplify the coding sequence of the complete variable region and the first constant domain of immunoglobulin heavy chains.
S Y Chang +3 more
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We have developed PCR primers for the amplification and cloning of the genes encoding human antibody fragments. Two sets of primers were designed to amplify the coding sequence of the complete variable region and the first constant domain of immunoglobulin heavy chains.
S Y Chang +3 more
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Caries Research, 1984
Immunoglobulin A (IgA) protease, a family of bacterial enzymes, cleaves human IgA1 at a single bond generating distinct Fab and Fc fragments. Purified secretory IgA with known specificity for Streptococcus mutans NCTC 10449 (serotype c) was hydrolyzed with IgA protease prepared from Streptococcus sanguis ATCC 10556.
C. P. Mallett +2 more
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Immunoglobulin A (IgA) protease, a family of bacterial enzymes, cleaves human IgA1 at a single bond generating distinct Fab and Fc fragments. Purified secretory IgA with known specificity for Streptococcus mutans NCTC 10449 (serotype c) was hydrolyzed with IgA protease prepared from Streptococcus sanguis ATCC 10556.
C. P. Mallett +2 more
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Crystal structure of human immunoglobulin fragment Fab new refined at 2.0 Å esolution
Proteins: Structure, Function, and Bioinformatics, 1992AbstractThe three‐dimensional structure of the human immunoglobulin fragment Fab New (IgG1,λ) has been refined to a crystal‐lographic R‐factor of 16.9% to 2Å resolution. Rms deviations of the final model from ideal geometry are 0.014 Å for bond distances and 3.03° for bond angles.
Frederick Saul, Roberto J. Poljak
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Molecular Immunology, 1981
Abstract Papain-derived fragments (Fab and Fc) were used to localize previously uncharacterized chicken 7S immunoglobulin (Ig§) allotypic specificities (G-1.7, G-1.8, G-1.9, G-1.10, and G-1.12). Based on the molar amounts of Fab and Fc preparations relative to undigested 7S Ig to inhibit 50% of binding of 125 I-7S Ig with homologous alloantiserum ...
Lean Kuan Ch'ngi, Albert A. Benedict
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Abstract Papain-derived fragments (Fab and Fc) were used to localize previously uncharacterized chicken 7S immunoglobulin (Ig§) allotypic specificities (G-1.7, G-1.8, G-1.9, G-1.10, and G-1.12). Based on the molar amounts of Fab and Fc preparations relative to undigested 7S Ig to inhibit 50% of binding of 125 I-7S Ig with homologous alloantiserum ...
Lean Kuan Ch'ngi, Albert A. Benedict
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Biochemistry, 1976
The conformational equilibria and the kinetics of the approach to equilibrium of an IgG1 myeloma (Wes) Fab fragment (SSFab) and its mildly reduced and S-carboxyamidomethylated derivative (RAFab) were studied as a function of guanidine hydrochloride concentration.
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The conformational equilibria and the kinetics of the approach to equilibrium of an IgG1 myeloma (Wes) Fab fragment (SSFab) and its mildly reduced and S-carboxyamidomethylated derivative (RAFab) were studied as a function of guanidine hydrochloride concentration.
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Gene, 1993
We have combined the high cloning efficiency of the lambda bacteriophage vectors with the surface expression screening method for the display of combinatorial antibody fragment (Fab) libraries on the surface of filamentous phage particles. The utility of the herein described ImmunoZAP 13 system for the isolation of Fabs that specifically bind antigen ...
Amy E. Lovejoy +4 more
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We have combined the high cloning efficiency of the lambda bacteriophage vectors with the surface expression screening method for the display of combinatorial antibody fragment (Fab) libraries on the surface of filamentous phage particles. The utility of the herein described ImmunoZAP 13 system for the isolation of Fabs that specifically bind antigen ...
Amy E. Lovejoy +4 more
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Production and purification of Fab′ fragments from chicken egg yolk immunoglobulin Y (IgY)
Journal of Immunological Methods, 1993Methods were described for the production of Fab and Fab' fragments from chicken egg yolk IgY also referred to as IgG by papain and pepsin digestion respectively. Pepsin digestion was found to be suitable for the large scale preparation and purification of Fab'.
Shuryo Nakai, E. M. Akita
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