Search results
Results from the WOW.Com Content Network
A ribosome-inactivating protein (RIP) is a protein synthesis inhibitor that acts at the eukaryotic ribosome. [2] This protein family describes a large family of such proteins that work by acting as rRNA N-glycosylase (EC 3.2.2.22).
Saporin / ˈ s æ p ə r ɪ n / is a protein that is useful in biological research applications, especially studies of behavior. Saporins are so-called ribosome inactivating proteins (RIPs), due to its N-glycosidase activity, from the seeds of Saponaria officinalis (common name: soapwort).
Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from eukaryotic ribosomes. Ricin A-chain and related toxins show this activity. The only protein family known to have this activity is the ribosome-inactivating protein (RIP) family.
Ricin is the best known representative of the ribosomal inactivating protein (RIP) family. [22] RIPs are also highly specialized toxic proteins produced by plants and fungi that inactivate ribosomes acting as N-glycosidases. Its target is found in the same singular structure of the rRNA that is attacked by ribotoxins.
Volkensin is a galactose specific lectin that can inhibit protein synthesis in whole cells and in cell-free lysates. This protein can be included into the category of risin like toxins and it resembles modeccin, the toxin of Adenia digitata. Although very similar in composition, volkensin contains more cysteine residues and more than twice as ...
Trichosanthin is a ribosome-inactivating protein. [1] [2] It is derived from Trichosanthes kirilowii. [3] It is also an abortifacient. [4] References
Main page; Contents; Current events; Random article; About Wikipedia; Contact us; Pages for logged out editors learn more
EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome.It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome.