The effect of cosolutes on the isomerization of aspartic acid residues and conformational stability in a monoclonal antibody

2007 ◽  
Vol 96 (7) ◽  
pp. 1708-1718 ◽  
Author(s):  
Aditya A. Wakankar ◽  
J.u.n. Liu ◽  
David VanderVelde ◽  
Y.John Wang ◽  
Steven J. Shire ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Aspartic Acid ◽  
Conformational Stability

High-throughput determination of free d-aspartic acid in mammals by enzyme immunoassay using specific monoclonal antibody

2006 ◽  
Vol 357 (1) ◽  
pp. 15-20 ◽  
Author(s):  
Tomohiro Ohgusu ◽  
Kenji Hamase ◽  
Hiroyuki Tanaka ◽  
Yukihiro Shoyama ◽  
Kiyoshi Zaitsu
Keyword(s):  
Monoclonal Antibody ◽  
Enzyme Immunoassay ◽  
Aspartic Acid ◽  
High Throughput ◽  
Specific Monoclonal Antibody

Local Dynamics and Their Alteration by Excipients Modulate the Global Conformational Stability of an lgG1 Monoclonal Antibody

2012 ◽  
Vol 101 (12) ◽  
pp. 4444-4457 ◽  
Author(s):  
Santosh V. Thakkar ◽  
Jae Hyun Kim ◽  
Hardeep S. Samra ◽  
Hasige A. Sathish ◽  
Steven M. Bishop ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Conformational Stability ◽  
Local Dynamics

The monoclonal antibody TAL16.1 recognizes the aspartic acid residue at position 70 in DRB gene products

1993 ◽  
Vol 41 (1) ◽  
pp. 42-46 ◽  
Author(s):  
A. M. Sadler ◽  
J. M. Heyes ◽  
S. G. E. Marsh ◽  
P. Krausa ◽  
G. E. Reynolds ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Aspartic Acid ◽  
Gene Products ◽  
Aspartic Acid Residue ◽  
Drb Gene

Effects of Salts from the Hofmeister Series on the Conformational Stability, Aggregation Propensity, and Local Flexibility of an IgG1 Monoclonal Antibody

Biochemistry ◽  
2013 ◽  
Vol 52 (19) ◽  
pp. 3376-3389 ◽  
Author(s):  
Ranajoy Majumdar ◽  
Prakash Manikwar ◽  
John M. Hickey ◽  
Hardeep S. Samra ◽  
Hasige A. Sathish ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Conformational Stability ◽  
Hofmeister Series ◽  
Aggregation Propensity ◽  
Igg1 Monoclonal Antibody ◽  
Local Flexibility

scholarly journals Substitution at Aspartic Acid 1128 in the SARS Coronavirus Spike Glycoprotein Mediates Escape from a S2 Domain-Targeting Neutralizing Monoclonal Antibody

PLoS ONE ◽  
2014 ◽  
Vol 9 (7) ◽  
pp. e102415 ◽  
Author(s):  
Oi-Wing Ng ◽  
Choong-Tat Keng ◽  
Cynthia Sau-Wai Leung ◽  
J. S. Malik Peiris ◽  
Leo Lit Man Poon ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Aspartic Acid ◽  
Sars Coronavirus ◽  
Spike Glycoprotein ◽  
Neutralizing Monoclonal Antibody

scholarly journals Molecular Basis for Species and Ligand Specificity of a Monoclonal Antibody Raised Against Human IGF-I

Endocrinology ◽  
1997 ◽  
Vol 138 (10) ◽  
pp. 4521-4523 ◽  
Author(s):  
Judson J. Van Wyk ◽  
Eyvonne T. Bruton
Keyword(s):  
Monoclonal Antibody ◽  
Aspartic Acid ◽  
Molecular Basis ◽  
Ligand Specificity ◽  
Critical Importance ◽  
High Concentration ◽  
Igf I ◽  
Very High

Abstract The anti-hIGF-I monoclonal antibody, α-sm1.2, was found to have substantial crossreactivity with human and rat IGF-II, but recognized rat IGF-I only when this ligand was present at very high concentration. (E50 for hIGF-I ∼3.5 ng/tube vs. ∼12,000 ng/tube for rat IGF-I). In the context of previous studies to define the epitope(s) of α-sm1.2, these findings point to the critical importance of aspartic acid at residue 20 in the B domain in determining the species and ligand specificity of this antibody. Previous studies using this antibody in rodent tissues may require reinterpretation in the light of these findings.

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