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New coupling agents for the synthesis of immunotoxins containing a hindered disulfide bond with improved stability in vivo.
In conclusion, immunotoxins prepared with the new coupling agents should have improved antitumor activity in vivo because they are longer lived and do not break down so readily to release free antibody which could compete for the target antigens.
Biochemical, cytotoxic and pharmacokinetic properties of an immunotoxin composed of a mouse monoclonal antibody Fib75 and the ribosome-inactivating protein alpha-sarcin from Aspergillus giganteus.
- E. Wawrzynczak, R. Henry, A. Cumber, G. Parnell, E. Derbyshire, N. Ulbrich
- BiologyEuropean journal of biochemistry
- 1 February 1991
An immunotoxin was synthesized by the attachment of alpha-sarcin, the ribosome-inactivating protein derived from the mould Aspergillus giganteus, to a monoclonal mouse IgG2 antibody Fib75. The…
Antibody toxin conjugates: a perspective.
Comparative stabilities in vitro and in vivo of a recombinant mouse antibody FvCys fragment and a bisFvCys conjugate.
- A. Cumber, E. Ward, G. Winter, G. Parnell, E. Wawrzynczak
- Biology, ChemistryJournal of immunology
- 1 July 1992
A murine antibody FvCys fragment with a single additional cysteine residue at the C terminus of the VH domain was expressed in Escherichia coli from a modified expression plasmid containing the…
Selective cytotoxic effects of a ricin A chain immunotoxin made with the monoclonal antibody SWA11 recognising a human small cell lung cancer antigen.
The potential of mouse monoclonal antibodies for recognising different antigens associated with human small cell lung cancer (SCLC) to form active immunotoxins was assessed by an indirect in vitro…
Blood clearance in the rat of a recombinant mouse monoclonal antibody lacking the N-linked oligosaccharide side chains of the CH2 domains.
An anti‐mucin immunotoxin BrE‐3‐ricin A‐chain is potently and selectively toxic to human small‐cell lung cancer
The findings suggest that anti‐mucin immunotoxins may have a therapeutic role to play in the treatment of SCLC.
Antibodies to the protein core of the small cell lung cancer workshop antigen cluster‐w4 and to the leucocyte workshop antigen CD24 recognize the same short protein sequence leucine‐alanine‐proline
To determine the exact epitopes recognized by these MoAbs, an epitope mapping assay using peptides synthesized onto polyethylene pins was established and recognized the same short leucine‐alanine‐proline (LAP) sequence in an area without potential glycosylation sites close to the GPI anchor of the protein core of the cluster‐w4/CD24 antigen.
Molecular and biological properties of an abrin A chain immunotoxin designed for therapy of human small cell lung cancer.
- E. Wawrzynczak, U. Zangemeister‐Wittke, R. Stahel
- Biology, ChemistryBritish Journal of Cancer
- 1 August 1992
The results of this study indicate that the antigen recognised by SWA11 is an effective target for therapy of SCLC with A chain ITs in vivo.