Measurement of blood holoceruloplasmin by EIA using a mouse monoclonal antibody directed to holoceruloplasmin. Implication for mass screening of Wilson disease

1994 ◽  
Vol 17 (5) ◽  
pp. 616-620 ◽  
Author(s):  
F. Endo ◽  
K. Taketa ◽  
K. Nakamura ◽  
H. Awata ◽  
A. Tanoue ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mass Screening ◽  
Wilson Disease ◽  
Mouse Monoclonal Antibody

Phase I trial of chimeric (human-mouse) monoclonal antibody L6 in patients with non-small-cell lung, colon, and breast cancer

1993 ◽  
Vol 36 (4) ◽  
pp. 267-273 ◽  
Author(s):  
Gary E. Goodman ◽  
Ingegerd Hellstrom ◽  
Dale E. Yelton ◽  
James L. Murray ◽  
Sarah O'Hara ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Monoclonal Antibody ◽  
Phase I ◽  
Phase I Trial ◽  
Small Cell ◽  
Mouse Monoclonal Antibody ◽  
Small Cell Lung

scholarly journals Value in Development of a TAPIR-Like Mouse Monoclonal Antibody to Aβ

2008 ◽  
Vol 14 (2) ◽  
pp. 175-177 ◽  
Author(s):  
Kumar Sambamurti ◽  
Miguel A. Pappolla ◽  
K.S. Jagannatha Rao
Keyword(s):  
Monoclonal Antibody ◽  
Mouse Monoclonal Antibody

Definition of Essential Amino Acid Residues in the Recognition of a Peptide by a Mouse Monoclonal Antibody

1997 ◽  
Vol 52 (3-4) ◽  
pp. 274-278
Author(s):  
Laura Rosanó ◽  
Francesca Di Modugno ◽  
Giulia Romagnoli ◽  
Alberto Chersi
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Critical Role ◽  
Binding Activity ◽  
Mouse Monoclonal Antibody ◽  
Amino Acid Residues ◽  
Binding Data ◽  
Amino Acid Stretch ◽  
Definition Of ◽  
Key Residues

AbstractA mouse monoclonal antibody reacting in ELISA with a synthetic peptide representing a linear amino acid stretch of the protein antigen was tested on all overlap­ ping 5-mer to 9-mer fragments of the peptide, as prepared by multi-pin synthesis. Analysis of the binding data suggests that several residues in the peptide might be relatively unrelevant for recognition, while few others seem to play a critical role as key residues. On the basis of such observations, we attempted to reconstruct an alternative essential epitope by introducing multiple amino acid substitutions in the 9-mer peptide exhibiting the best binding activity, and then tested its ability to be recognized by the monoclonal antibody.

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