Influence of temperature and pH on the antigen-binding capacity of immunoglobulin G in cheese whey derived from hyper-immune milk

2014 ◽  
Vol 37 (2) ◽  
pp. 111-116 ◽  
Author(s):  
Francisco Riera ◽  
Alejandro Álvarez
Keyword(s):  
Immunoglobulin G ◽  
Cheese Whey ◽  
Binding Capacity ◽  
Antigen Binding ◽  
Influence Of Temperature

scholarly journals Production of Recombinant Monoclonal Antibodies in the Egg White of Gene-Targeted Transgenic Chickens

Genes ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 38
Author(s):  
Takehiro Mukae ◽  
Sho Okumura ◽  
Takuma Watanobe ◽  
Kyoko Yoshii ◽  
Takahiro Tagami ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Capacity ◽  
Specific Binding ◽  
Egg White ◽  
Peptide Sequence ◽  
Efficient Production ◽  
Antigen Binding ◽  
Transgenic Chicken ◽  
Bioreactor System ◽  
Transgenic Chickens

Increased commercial demand for monoclonal antibodies (mAbs) has resulted in the urgent need to establish efficient production systems. We previously developed a transgenic chicken bioreactor system that effectively produced human cytokines in egg whites using genome-edited transgenic chickens. Here, we describe the application of this system to mAb production. The genes encoding the heavy and light chains of humanized anti-HER2 mAb, linked by a 2A peptide sequence, were integrated into the chicken ovalbumin gene locus using a CRISPR/Cas9 protocol. The knock-in hens produced a fully assembled humanized mAb in their eggs. The mAb expression level in the egg white was 1.4–1.9 mg/mL, as determined by ELISA. Furthermore, the antigen binding affinity of the anti-HER2 mAb obtained was estimated to be equal to that of the therapeutic anti-HER2 mAb (trastuzumab). In addition, antigen-specific binding by the egg white mAb was demonstrated by immunofluorescence against HER2-positive and -negative cells. These results indicate that the chicken bioreactor system can efficiently produce mAbs with antigen binding capacity and can serve as an alternative production system for commercial mAbs.

Development of viper-venom antibodies in chicken egg yolk and assay of their antigen binding capacity

Toxicon ◽  
2002 ◽  
Vol 40 (7) ◽  
pp. 857-861 ◽  
Author(s):  
C Maya Devi ◽  
M Vasantha Bai ◽  
L.K Krishnan
Keyword(s):  
Binding Capacity ◽  
Egg Yolk ◽  
Antigen Binding ◽  
Chicken Egg ◽  
Chicken Egg Yolk

Cyclic peptide ligand with high binding capacity for affinity purification of immunoglobulin G

2016 ◽  
Vol 1466 ◽  
pp. 105-112 ◽  
Author(s):  
Hyo Jin Kang ◽  
Weonu Choe ◽  
Jeong-Ki Min ◽  
Young-mi Lee ◽  
B. Moon Kim ◽  
...  
Keyword(s):  
Immunoglobulin G ◽  
Cyclic Peptide ◽  
Binding Capacity ◽  
Affinity Purification ◽  
Peptide Ligand ◽  
High Binding

A Radioimmunoassay of the Antigen-Binding Capacity of Rabbit Antiserum Prepared with Axenically Grown Entamoeba histolytica, Laredo Strain

1973 ◽  
Vol 59 (5) ◽  
pp. 927 ◽  
Author(s):  
Bernard Halpern ◽  
Richard A. Albach ◽  
James G. Shaffer ◽  
Ralph E. Dolkart
Keyword(s):  
Entamoeba Histolytica ◽  
Binding Capacity ◽  
Rabbit Antiserum ◽  
Antigen Binding

scholarly journals Recombinant Escherichia coli Strain Produces a ZZ Domain Displaying Biopolyester Granules Suitable for Immunoglobulin G Purification

2006 ◽  
Vol 72 (11) ◽  
pp. 7394-7397 ◽  
Author(s):  
Jane A. Brockelbank ◽  
Verena Peters ◽  
Bernd H. A. Rehm
Keyword(s):  
Escherichia Coli ◽  
Immunoglobulin G ◽  
Binding Capacity ◽  
Protein A ◽  
Coli Strain ◽  
Pha Synthase ◽  
Enzyme Linked Immunosorbent Assay ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
Igg Binding

ABSTRACT The immunoglobulin G (IgG) binding ZZ domain of protein A from Staphylococcus aureus was fused to the N terminus of the polyhydroxyalkanoate (PHA) synthase from Cupriavidus necator. The fusion protein was confirmed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and mediated formation of ZZ domain-displaying PHA granules in recombinant Escherichia coli. The IgG binding capacity of isolated granules was assessed using enzyme-linked immunosorbent assay and could be enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient purification of IgG from human serum.

scholarly journals 131I anti-CD45 radioimmunotherapy effectively targets and treats T-cell non-Hodgkin lymphoma

Blood ◽  
2009 ◽  
Vol 113 (23) ◽  
pp. 5905-5910 ◽  
Author(s):  
Ajay K. Gopal ◽  
John M. Pagel ◽  
Jonathan R. Fromm ◽  
Shani Wilbur ◽  
Oliver W. Press
Keyword(s):  
T Cell ◽  
Complete Remission ◽  
Tumor Targeting ◽  
Binding Capacity ◽  
Antigen Binding ◽  
Clinical Use ◽  
Non Hodgkin Lymphoma ◽  
Biodistribution Studies ◽  
Remission Rates ◽  
Liver And Kidney

AbstractRadioimmunotherapy (RIT) options for T-cell non-Hodgkin lymphomas (T-NHLs) are limited. We evaluated anti-CD45-RIT in human (h) and murine (m) T-NHL. CD45 was highly expressed on hT-NHL patient samples (median, 2.3 × 105 antigen-binding capacity units/cell) and hT-NHL cell lines (3.4 × 105 CD45 antigen-binding capacity units/cell). Biodistribution studies in hTNHL xenografts showed that 131I-labeled BC8 (anti-hCD45) delivered 154% (P = .01) and 237% (P = .002) more radioiodine to tumor sites over control antibodies at 24 hours and 48 hours, respectively. Importantly, tumor sites targeted with 131I-BC8 exhibited 2.5-fold (P = .05), 3.0-fold (P = .007), and 3.6-fold (P = .07) higher 131I retention over the nontarget organs of lungs, liver, and kidneys, respectively (24 hours). Because the clinical use of anti-hCD45 would target both T-NHL and other hematolymphoid tissues, we evaluated the ability of anti-mCD45 to target mT-NHL. mT-NHL grafts targeted with anti-mCD45 correspondingly retained 5.3 (P < .001), 5.4 (P < .001), and 8.7 (P < .001) times the radioactivity in tumor sites compared with nontarget organs of lung, liver, and kidney. 131I-labeled BC8 therapy yielded improved complete remission rates (75% vs 0%, P < .001) and progression-free survivals (median, 23 days vs 4.5 days, P < .001) compared with controls. These data indicate that the high CD45 expression of T-NHL allows reliable tumor targeting and disease control supporting anti-CD45 RIT for T-NHL patients.

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