Production and Characterization of a Recombinant Camel Full Heavy Chain Antibody against Human IgE

2015 ◽  
Vol 8 (4) ◽  
pp. 257-262
Author(s):  
Sana’ H. Yousef ◽  
Abdelrahman M. Rawashdeh ◽  
Raida W. Khalil
Keyword(s):  
Heavy Chain ◽  
Heavy Chain Antibody

Isolation and Characterization of a Thermally Stable Recombinant Anti-Caffeine Heavy-Chain Antibody Fragment

2006 ◽  
Vol 78 (13) ◽  
pp. 4501-4508 ◽  
Author(s):  
Ruth C. Ladenson ◽  
Dan L. Crimmins ◽  
Yvonne Landt ◽  
Jack H. Ladenson
Keyword(s):  
Heavy Chain ◽  
Antibody Fragment ◽  
Thermally Stable ◽  
Isolation And Characterization ◽  
Heavy Chain Antibody

scholarly journals Gamma heavy chain disease: clinical aspects and characterization of a deleted, noncovalently linked gamma1 heavy chain dimer (BAZ)

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 495-505 ◽  
Author(s):  
GB Faguet ◽  
BP Barton ◽  
LL Smith ◽  
FA Garver
Keyword(s):  
Heavy Chain ◽  
Plasma Cells ◽  
Clinical Feature ◽  
Clinical Aspects ◽  
Submaxillary Glands ◽  
Underlying Malignancy ◽  
V Region ◽  
Allotypic Marker ◽  
Heavy Chain Disease

Abstract This report describes the clinical and immunoglobulin features of a patient with gamma heavy chain disease (HCD), who presented with a clinical picture suggestive of an underlying malignancy rather than the usual picture of lymphoma or granulomatous disease. A unique clinical feature was the nearly total replacement of the submaxillary glands by plasma cells. The patient's serum and urine contained a paraprotein, gammaHCD protein BAZ, which belongs to the gamma1 subclass and forms noncovalently linked dimers with a molecular weight of approximately 60,000 daltons. This mutant protein exhibited a deletion which encompassed most of the variable (V) region, the first constant domain (CH 1), and the hinge region. In addition, preliminary structural analyses demonstrated the replacement of alanine by glycine in position 431 of the carboxyterminal octadecapeptide. This substitution may possibly represent another allotypic marker on IgG1 proteins.

scholarly journals Characterization of a strong positive cis-acting element of the human beta-myosin heavy chain gene in fetal rat heart cells.

1992 ◽  
Vol 267 (14) ◽  
pp. 9917-9924 ◽  
Author(s):  
I.L. Flink ◽  
J.G. Edwards ◽  
J.J. Bahl ◽  
C.C. Liew ◽  
M Sole ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Rat Heart ◽  
Chain Gene ◽  
Heart Cells ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene ◽  
Cis Acting ◽  
Fetal Rat ◽  
Rat Heart Cells

scholarly journals Inversions produced during V(D)J rearrangement at IgH, the immunoglobulin heavy-chain locus.

1995 ◽  
Vol 15 (2) ◽  
pp. 671-681 ◽  
Author(s):  
A E Sollbach ◽  
G E Wu
Keyword(s):  
Heavy Chain ◽  
Adult Mouse ◽  
Fetal Liver ◽  
Immunoglobulin Heavy Chain ◽  
Antigen Receptors ◽  
Adult Mice ◽  
Chain Locus ◽  
Heavy Chain Locus ◽  
Fetal Liver Cells

Diversity in immunoglobulin antigen receptors is generated in part by V(D)J recombination. In this process, different combinations of gene elements are joined in various configurations. Products of V(D)J recombination are coding joints, signal joints, and hybrid junctions, which are generated by deletion or inversion. To determine their role in the generation of diversity, we have examined two sorts of recombination products, coding joints and hybrid junctions, that have formed by inversion at the mouse immunoglobulin heavy-chain locus. We developed a PCR assay for quantification and characterization of inverted rearrangements of DH and JH gene elements. In primary cells from adult mice, inverted DJH rearrangements are detectable but they are rare. There were approximately 1,100 to 2,200 inverted DJH coding joints and inverted DJH hybrid junctions in the marrow of one adult mouse femur. On day 16 of gestation, inverted DJH rearrangements are more abundant. There are approximately 20,000 inverted DJH coding joints and inverted DJH hybrid junctions per day 16 fetal liver. In fetal liver cells, the number of inverted DJH rearrangements remains relatively constant from day 14 to day 16 of gestation. Inverted DJH rearrangements to JH4, the most 3' JH element, are more frequently detected than inverted DJH rearrangements to other JH elements. We compare the frequencies of inverted DJH rearrangements to previously determined frequencies of uninverted DJH rearrangements (DJH rearrangements formed by deletion). We suggest that inverted DJH rearrangements are influenced by V(D)J recombination mechanistic constraints and cellular selection.

scholarly journals Characterization of a Temperature-Sensitive Vertebrate Clathrin Heavy Chain Mutant as a Tool to Study Clathrin-Dependent Events In Vivo

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12017 ◽  
Author(s):  
Petra Neumann-Staubitz ◽  
Stephanie L. Hall ◽  
Joseph Kuo ◽  
Antony P. Jackson
Keyword(s):  
Heavy Chain ◽  
Temperature Sensitive ◽  
Clathrin Heavy Chain
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