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Luffin‐S—a small novel ribosome‐inactivating protein from Luffa cylindrica
Author(s) -
Gao Wenda,
Ling Jun,
Zhong Xuemei,
Liu Wangyi,
Zhang auHailing Yang Ruping,
Cao Huiting,
Zhang Zuchuan
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00554-0
Subject(s) - ribosome inactivating protein , immunotoxin , ribosome , protein biosynthesis , chemistry , moiety , ricin , rna , biochemistry , stereochemistry , toxin , cytotoxicity , gene , in vitro
We purified and characterized a novel RIP (ribosome inactivating protein), Luffin‐S from the seeds of Luffa cylindrica . Different from Luffin‐A and B, which are RNA N ‐glycosidases with molecular weights of 27 and 28 kDa, respectively, Luffin‐S has an M.W. of only approx. 10 kDa, much smaller than any other RIPs so far investigated. Its abundant resources, toxicity similar to TCS in a cell‐free protein synthesis system and unique mechanism as phosphodiesterase, like α‐sarcin, promisingly make it a potential toxic moiety of immunotoxin.