Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody
- 1 October 1993
- journal article
- Published by Elsevier in Molecular Immunology
- Vol. 30 (15) , 1361-1367
- https://doi.org/10.1016/0161-5890(93)90097-u
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Chimeric and humanized antibodies with specificity for the CD33 antigen.The Journal of Immunology, 1992
- A phase I trial of monoclonal antibody M195 in acute myelogenous leukemia: specific bone marrow targeting and internalization of radionuclide.Journal of Clinical Oncology, 1991
- NMR-derived model for a peptide-antibody complexBiochemistry, 1990
- Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineeringProtein Engineering, Design and Selection, 1990
- Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region.The Journal of Immunology, 1989
- Glycosylation of a VH residue of a monoclonal antibody against alpha (1----6) dextran increases its affinity for antigen.The Journal of Experimental Medicine, 1988
- The L4F3 antigen is expressed by unipotent and multipotent colony- forming cells but not by their precursorsBlood, 1986
- A monoclonal antibody reactive with normal and leukemic human myeloid progenitor cellsLeukemia Research, 1984
- Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-.ANG. resolutionBiochemistry, 1981
- Carbohydrate content of fragments and polypeptide chains of human .gamma.G-myeloma proteins of different heavy-chain subclassesBiochemistry, 1968