Immuno-detection of pokeweed antiviral protein




Lee, Matthew Chien-Hung

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Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein isolated from the leaves of Phytolacca americana. It belongs to a larger family of proteins known as ribosome inactivating proteins (RIPs). These proteins enzymatically function as ribosome-specific N-glycosidases by removing a single adenine from the larger subunit of animal and plant ribosomes. It has been proposed that RIPs are defensive proteins which protect the host plant from invading organisms. Aside from being an biological curiosity, the enzymatic activity of PAP has found practical applications in the formulation of immunotoxins that are currently being tested for their anticancer and antiviral efficacy. During purification, a number of different forms of PAP have been identified: the original PAP from spring leaves, PAP-II from summer leaves, and P AP-S from the seeds of Phytolacca americana, among which PAP-II was of particular interest to us. Affinity-purified rabbit antibodies against PAP and PAP-II were developed and used in enzyme linked immunosorbent assay (ELISA), Western blot and slot blot detection of PAP and PAP-II in crude samples as well as samples at various stages of purification.



pokeweed, antiviral proteins, antibodies


Lee, M. C. H. (1999). Immuno-detection of pokeweed antiviral protein (Unpublished thesis). Southwest Texas State University, San Marcos, Texas.


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