[Purification and partial characterization of luffin P1, a peptide with translational inhibitory activity and trypsin inhibitory activity, from seeds of Luffa cylindrica].

A peptide, luffin P1, from seeds of Luffa cylindrica, was purified by ammonia sulfate precipitation, CM-52 ion exchange chromatography, Blue-gel affinity chromatography and FPLC Mono S ion exchange chromatography. Its molecular weight was 5226.5 as determined by MALDI-TOF-MS analysis.

[Purification and characterization of trichokirin-S1, a novel ribosome-inactivating peptide from seeds of Trichosanthes kirilowii].

A novel peptide from the seeds of Trichosanthes kirilowii, trichokirin-S1, was purified by extraction of protein body, ammonia sulfate precipitation, Blue-gel affinity chromatography, FPLC Mono S ion exchange chromatography and Superose12 gel filtration chromatography. Its molecular weight was determined to be 11,426 by MALDI-TOF MS analysis. Its reaction mechanism to inactive ribosome was the same as that of the ribosome-inactivating protein trichosanthin, a rRNA N-glycosidase.

Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica.

A peptide designated Luffin P1 was purified from the seeds of Luffa cylindrica. Its molecular mass was determined to be 5226.1 Da by MALDI-TOF MS analysis.