| Literature DB >> 11853228 |
Abstract
A ribosome inactivating peptide, with an N-terminal sequence exhibiting pronounced similarity to that of the 6.5 kDa-arginine/glutamate-rich polypeptide from Luffa cylindrica seeds, was isolated from seeds of a closely related species, the ridge gourd Luffa acutangula. The 5.6 kDa-peptide designated luffangulin inhibited cell-free translation with an IC50 of 3.5 nM but lacked inhibitory activity toward HIV-1 reverse transcriptase. It was similar to luffaculin, the 28 kDa ribosome inactivating protein in being unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel. On CM-cellulose luffangulin and luffaculin appeared as two adjacent peaks.Entities:
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Year: 2002 PMID: 11853228 DOI: 10.1016/s0024-3205(01)01466-7
Source DB: PubMed Journal: Life Sci ISSN: 0024-3205 Impact factor: 5.037