These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins, unrelated in amino-acid sequence, from Petrocoptis species.
    Author: Arias FJ, Rojo MA, Ferreras JM, Iglesias R, Muñoz R, Soriano F, Méndez E, Barbieri L, Girbés T.
    Journal: Planta; 1994; 194(4):487-91. PubMed ID: 7528586.
    Abstract:
    Two new N-glycosidase type-1 ribosome-inactivating proteins (RIPs), denoted petroglaucin 1 and petrograndin, respectively, were isolated from the plants Petrocoptis glaucifolia (Lag.) Boiss sp. viscosa (Rothm.) Lainz and Petrocoptis grandiflora Rothm. These new RIPs do not share H2N-terminal amino-acid sequence homology with petroglaucin (now denoted as petroglaucin 2), the only other type-1 RIP to be isolated from P. glaucifolia (Arias et al. (1992) Planta 186, 532-540). Petroglaucin 1 shares amino-acid sequence homology with RIPs from Cucurbitaceae while petroglaucin 2 and petrograndin do so with saporins and dianthin 30 (Caryophyllaceae). The new RIPs strongly inhibited protein synthesis at subnanomolar concentrations in rabbit reticulocyte lysates and other eukaryotic cell-free systems, but they were inactive on bacterial ribosomes.
    [Abstract] [Full Text] [Related] [New Search]