scholarly journals Tailored amino acid diversity for the evolution of antibody affinity

mAbs ◽  
2012 ◽  
Vol 4 (6) ◽  
pp. 664-672 ◽  
Author(s):  
Andrea González-Muñoz ◽  
Evert Bokma ◽  
Desmond O’Shea ◽  
Kevin Minton ◽  
Martin Strain ◽  
...  
1981 ◽  
Vol 197 (3) ◽  
pp. 629-636 ◽  
Author(s):  
J L McKenzie ◽  
A K Allen ◽  
J W Fabre

Human and canine brain Thy-1 antigens were solubilized in deoxycholate and antigen activity was followed both by conventional absorbed anti-brain xenosera of proven specificity and by mouse monoclonal antibodies to canine and human Thy-1. It is shown that greater than 80% of Thy-1 activity in the dog and man binds to lentil lectin, that the mobility on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of canine and human Thy-1 is identical with that of rat Thy-1 and that the Stokes radius in deoxycholate of canine and human brain Thy-1 is 3.0 nm and 3.25 nm respectively. Both lentil lectin affinity chromatography followed by gel-filtration chromatography on the one hand and monoclonal antibody affinity chromatography on the other gave high degrees of purification of the brain Thy-1 molecule in the dog and man, resulting in single bands staining for both protein and carbohydrate on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (except for a slight contaminant of higher molecular weight staining for protein but not carbohydrate with human Thy-1 purified by lentil lectin and gel-filtration chromatography). Analysis of canine and human brain Thy-1 purified by monoclonal antibody affinity chromatography with additional gel filtration through Sephadex G-200 showed that these molecules had respectively 38% and 36% carbohydrate. The amino acid and carbohydrate compositions were similar to those previously reported for Thy-1 of the rat and mouse, the main point of interest being the presence in canine and human brain Thy-1 of N-acetylgalactosamine, which has been reported in rat and mouse brain Thy-1 but not in Thy-1 from other tissues.


2007 ◽  
Vol 81 (1) ◽  
pp. 44-52 ◽  
Author(s):  
David Hamm ◽  
Brian S. Mautz ◽  
Mariana F. Wolfner ◽  
Charles F. Aquadro ◽  
Willie J. Swanson

2008 ◽  
Vol 381 (2) ◽  
pp. 407-418 ◽  
Author(s):  
Ryan N. Gilbreth ◽  
Kaori Esaki ◽  
Akiko Koide ◽  
Sachdev S. Sidhu ◽  
Shohei Koide

2018 ◽  
Vol 42 (2) ◽  
pp. e32-e34 ◽  
Author(s):  
Paul Rémi Petit ◽  
Patrick Borentain ◽  
Sarah Aherfi ◽  
Alban Benezech ◽  
Danielle Botta-Fridlund ◽  
...  

Genetics ◽  
2004 ◽  
Vol 166 (3) ◽  
pp. 1517-1527 ◽  
Author(s):  
Laura E. Rose ◽  
Peter D. Bittner-Eddy ◽  
Charles H. Langley ◽  
Eric B. Holub ◽  
Richard W. Michelmore ◽  
...  

2019 ◽  
Vol 2019 ◽  
pp. 1-28 ◽  
Author(s):  
Enéas Ricardo Konzen ◽  
Gustavo Henrique Recchia ◽  
Fernanda Cassieri ◽  
Danielle Gregorio Gomes Caldas ◽  
Jorge C. Berny Mier y Teran ◽  
...  

We analyzed the nucleotide variability and the expression profile of DREB genes from common bean, a crop of high economic and nutritional value throughout the world but constantly affected by abiotic stresses in cultivation areas. As DREB genes have been constantly associated with abiotic stress tolerance, we systematically categorized 54 putative PvDREB genes distributed in the common bean genome. It involved from AP2 domain location and amino acid conservation analysis (valine at the 14th position) to the identification of conserved motifs within peptide sequences representing six subgroups (A-1 to A-6) of PvDREB proteins. Four genes (PvDREB1F, PvDREB2A, PvDREB5A, and PvDREB6B) were cloned and analyzed for their expression profiles under abiotic stresses and their nucleotide and amino acid diversity in genotypes of Andean and Mesoamerican origin, showing distinct patterns of expression and nucleotide variability. PvDREB1F and PvDREB5A showed high relative inducibilities when genotypes of common bean were submitted to stresses by drought, salt, cold, and ABA. PvDREB2A inducibility was predominantly localized to the stem under drought. PvDREB6B was previously described as an A-2 (DREB2) gene, but a detailed phylogenetic analysis and its expression profile clearly indicated it belongs to group A-6. PvDREB6B was found as a cold- and dehydration-responsive gene, mainly in leaves. Interestingly, PvDREB6B also showed a high nucleotide and amino acid diversity within its coding region, in comparison to the others, implicating in several nonsynonymous amino acid substitutions between Andean and Mesoamerican genotypes. The expression patterns and nucleotide diversity of each DREB found in this study revealed fundamental characteristics for further research aimed at understanding the molecular mechanisms associated with drought, salt, and cold tolerance in common bean, which could be performed based on association mapping and functional analyses.


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