A Site-specific Antibody Produced with a Novel Immunization Procedure by Induction of Tolerance to Cross-reacting Determinants and Its Utilization in Clinical Research

2015 ◽  
pp. 87-97
Author(s):  
Toshiyuki Hamaoka
Keyword(s):  
Clinical Research ◽  
Specific Antibody ◽  
Site Specific ◽  
Immunization Procedure ◽  
A Site ◽  
Induction Of Tolerance

scholarly journals A Case Study to Identify the Drug Conjugation Site of a Site-Specific Antibody-Drug-Conjugate Using Middle-Down Mass Spectrometry

2019 ◽  
Vol 30 (11) ◽  
pp. 2419-2429 ◽  
Author(s):  
Oscar Hernandez-Alba ◽  
Stéphane Houel ◽  
Steve Hessmann ◽  
Stéphane Erb ◽  
David Rabuka ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Specific Antibody ◽  
Antibody Drug Conjugate ◽  
Site Specific ◽  
Drug Conjugate ◽  
Drug Conjugation ◽  
A Site ◽  
Antibody Drug

scholarly journals Idiotypic cross-reactivity between antibodies of different specificities.

1978 ◽  
Vol 148 (6) ◽  
pp. 1488-1497 ◽  
Author(s):  
R Karol ◽  
M Reichlin ◽  
R W Noble
Keyword(s):  
Sickle Cell ◽  
Specific Antibody ◽  
Cross Reactivity ◽  
Beta Chain ◽  
Site Specific ◽  
Low Level ◽  
Human Adult ◽  
Hemoglobin Molecule ◽  
Adult Hemoglobin ◽  
A Site

Cross-idiotypic specificity has been demonstrated between antibody populations of different specificities using antibodies directed toward human sickle cell hemoglobin (HbS). A site-specific antibody directed toward the beta6-position of HbS, anti-Val, was used to elicit an anti-idiotypic response in rabbits. Using this anti-idiotypic serum, idiotypic cross-reactivity was demonstrated between antibody populations that bind to human adult hemoglobin (HbA). It was demonstrated that in the case of the goat antibodies, these idiotypically cross-reacting antibodies are directed towards the beta6-position of the hemoglobin molecule. However, they differ in their specificity, binding to this site on HbA, whereas anti-Val binds only to HbS. The sheep antibody populations directed toward HbS differ qualitatively from those of the goat. Using rabbit anti-idiotypic serum specific for sheep anti-Val, cross-reactivity could be demonstrated with antibodies directed toward the alpha-chain of the hemoglobin molecule, as well as the beta-chain. There was also a low level of cross-reactivity with antibodies from a goat immunized with HbA.

scholarly journals Targeted Delivery of LXR Agonist Using a Site-Specific Antibody–Drug Conjugate

2015 ◽  
Vol 26 (11) ◽  
pp. 2216-2222 ◽  
Author(s):  
Reyna K. V. Lim ◽  
Shan Yu ◽  
Bo Cheng ◽  
Sijia Li ◽  
Nam-Jung Kim ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Targeted Delivery ◽  
Antibody Drug Conjugate ◽  
Site Specific ◽  
Drug Conjugate ◽  
A Site ◽  
Antibody Drug

scholarly journals Generation and characterization of a site-specific antibody for SIRT1 O-GlcNAcylated at serine 549

Glycobiology ◽  
2018 ◽  
Vol 28 (7) ◽  
pp. 482-487 ◽  
Author(s):  
Hui Shan ◽  
Jiahui Sun ◽  
Minghui Shi ◽  
Xue Liu ◽  
Zhu Shi ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Site Specific ◽  
A Site

scholarly journals Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene.

1989 ◽  
Vol 9 (4) ◽  
pp. 1507-1512 ◽  
Author(s):  
H Zhu ◽  
H Conrad-Webb ◽  
X S Liao ◽  
P S Perlman ◽  
R A Butow
Keyword(s):  
Genetic Analysis ◽  
Rna Processing ◽  
Fold Increase ◽  
Functional Expression ◽  
Rrna Gene ◽  
Yeast Mitochondria ◽  
Wild Type ◽  
Site Specific ◽  
Var1 Gene ◽  
A Site

All mRNAs of yeast mitochondria are processed at their 3' ends within a conserved dodecamer sequence, 5'-AAUAAUAUUCUU-3'. A dominant nuclear suppressor, SUV3-I, was previously isolated because it suppresses a dodecamer deletion at the 3' end of the var1 gene. We have tested the effects of SUV3-1 on a mutant containing two adjacent transversions within a dodecamer at the 3' end of fit1, a gene located within the 1,143-base-pair intron of the 21S rRNA gene, whose product is a site-specific endonuclease required in crosses for the quantitative transmission of that intron to 21S alleles that lack it. The fit1 dodecamer mutations blocked both intron transmission and dodecamer cleavage, neither of which was suppressed by SUV3-1 when present in heterozygous or homozygous configurations. Unexpectedly, we found that SUV3-1 completely blocked cleavage of the wild-type fit1 dodecamer and, in SUV3-1 homozygous crosses, intron conversion. In addition, SUV3-1 resulted in at least a 40-fold increase in the amount of excised intron accumulated. Genetic analysis showed that these phenotypes resulted from the same mutation. We conclude that cleavage of a wild-type dodecamer sequence at the 3' end of the fit1 gene is essential for fit1 expression.

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