A novel ribosome-inactivating protein (RIP) designated α-kirilowin was isolated from the seeds of Trichosanthes kirilowii. The molecular weight of α-kirilowin was estimated by SDS-polyacrylamide gel electrophoresis to be 28800 Da, which is slightly larger than another previously characterized ribosome-inactivating protein, β-kirilowin. The amino-acid composition of α-kirilowin grossly resembled β-kirilowin and other ribosome-inactivating proteins isolated from T. kirilowii tissues, including trichokirin, trichosanthin and karasurin. Intense immunological cross-reactivity between the two kirilowins; was detected by immunodiffusion. The N-terminal sequence of α-kirilowin was identical to that of β-kirilowin at least in the first ten residues. Peptide fingerprinting indicated both kirilowins were closely related. Biological activities as determined by inhibition of protein synthesis in a cell-free system, suppression of [3H]-thymidine incorporation into mouse melanoma cells and induction of abortion in mice were very similar for both kirilowins. We propose that the size difference between α- and β-kirilowin is either due to a C-terminal extension in α-kirilowin or differences in glycosylation, or a combination of both.
|Number of pages
|International Journal of Peptide and Protein Research
|Published - 1996
Scopus Subject Areas
- Ribosome-inactivating proteins
- Trichosanthes kirilowii