Factor VIII polypeptide specificity of monoclonal anti-factor VIII antibodies
Article first published online: 7 JUL 2008
DOI: 10.1111/j.1365-2141.1988.tb02435.x
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How to Cite
Shima, M., Yoshioka, A., Nakai, H., Tanaka, I., Fujiwara, T., Terada, S., Imai, S. and Fukui, H. (1988), Factor VIII polypeptide specificity of monoclonal anti-factor VIII antibodies. British Journal of Haematology, 70: 63–69. doi: 10.1111/j.1365-2141.1988.tb02435.x
Publication History
- Issue published online: 7 JUL 2008
- Article first published online: 7 JUL 2008
- Recieved 19 September 1987; accepted for publication 3 March 1988
- Abstract
- References
- Cited By
Four monoclonal antibodies against factor VIII, NMC-VIII/1, NMC-VIII/2, NMC-VIII/3 and NMC-VIII/4, were produced. The first three antibodies were of the IgG1 immunoglobulin subclass, while the fourth was IgM. The affinity of each antibody for factor VIII was high and antifactor VIII clotting activity was detected in NMC-VIII/2, NMC-VIII/3 and NMC-VIII/4. NMC-VIII/1 had no inhibitory effect on factor VIII clotting activity. Immunoblotting using purified intact and thrombin-treated factor VIII identified the antibodies’factor VIII polypeptide specificities. With thrombin-treated factor VIII the factor VIII fragments for NMC-VIII/1 and NMC-VIII/2 were 80 kDa and 54 kDa, respectively, while both NMC-VIII/3 and NMC-VIII/4 recognised a 44 kDa fragment. With intact factor VIII, antibodies NMC-VIII/2-4 bound to polypeptides larger than 90 kDa, especially NMC-VIII/2, which reacted with a chain of 330 kDa thought to be a mature form of factor VIII protein. We also detected a mature form of factor VIII in hepatic sinusoidal endothelial cells by immunoperoxidase staining.
Identification of the factor VIII polypeptides bearing these fragments enabled us to clarify the localization of the factor VIII thrombin cleavage site, and suggested the existence of factor VIII in hepatic sinusoidal endothelial cells.

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