Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody

M195 is a murine monoclonal antibody that binds to the CD33 antigen and is being tested for the treatment of myeloid leukemia. Surprisingly, a complementarity determining region (CDR)-grafted, humanized M195 antibody displayed a several-fold higher binding affinity for the CD33 antigen than the orig...

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Veröffentlicht in:	Molecular immunology 1993-10, Vol.30 (15), p.1361-1367
Hauptverfasser:	Man Sung Co, Scheinberg, David A., Avdalovic, Nevenka M., Mcgraw, Kimberly, Vasquez, Max, Caron, Philip C., Queen, Cary
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antibodies, immunoglobulins Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - immunology Antibody Affinity Antigens, CD - immunology Antigens, Differentiation, Myelomonocytic - immunology Binding Sites, Antibody Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology Glycoproteins - immunology Immunoglobulin Variable Region - chemistry Models, Molecular Molecular immunology Molecular Sequence Data Monoclonal antibodies Protein Structure, Tertiary Recombinant Fusion Proteins - immunology Sialic Acid Binding Ig-like Lectin 3 Structure-Activity Relationship
Online-Zugang:	Volltext
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