Isolation and characterization of a novel ribosome-inactivating protein, beta-kirilowin, from the seeds of Trichosanthes kirilowii.
A novel ribosome-inactivating protein designated beta-kirilowin was isolated from the seeds of Trichosanthes kirilowii. The proteins exhibited strong abortifacient activity in pregnant mice and produced a single band after SDS-polyacrylamide gel electrophoresis with an apparent mol. wt. of 27,500 daltons. It was active in inhibiting the cell-free translation system with an ID50 of about 1.8 ng/ml. No cross-reactivity with trichosanthin could be detected by immunodiffusion. Sequence comparison of the first 10 residues of beta-kirilowin with ribosome-inactivating proteins isolated from T. kirilowii such as trichosanthin, trichokirin and karasurin indicated 70%, 60% and 70% identity, respectively.
Dong
T X
TX
Department of Biochemistry, Chinese University of Hong Kong, Shiantin, New Territories.
Ng
T B
TB
Yeung
H W
HW
Wong
R N
RN
D000019:Abortifacient Agents; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005260:Female; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000633:toxicity; D012270:Ribosomes / Q000187:drug effects*; D012639:Seeds / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000019:Abortifacient Agents; D000596:Amino Acids; D010940:Plant Proteins; C086066:beta-kirilowin protein, Trichosanthes kirilowii