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2 edition of Dianthin 30, a ribosome inactivating protein from Dianthus caryophyllus L. found in the catalog.

Dianthin 30, a ribosome inactivating protein from Dianthus caryophyllus L.

Giuseppe Antonio Legname

Dianthin 30, a ribosome inactivating protein from Dianthus caryophyllus L.

cDNA cloning and high level expression in Escherichia coli

by Giuseppe Antonio Legname

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Published by typescript in [s.l.] .
Written in English


Edition Notes

Thesis (Ph.D.) - University of Warwick, 1996.

StatementGiuseppe Antonio Legname.
The Physical Object
Pagination178p.
Number of Pages178
ID Numbers
Open LibraryOL17495950M

Doctor of Philosophy with a thesis entitled "Diant a ribosome inactivating protein from Dianthus caryophyllus", supervisor Professor J. Michael Lord at University of Warwick, Coventry, UK. Honors and Awards: Visiting Fellow at Warwick University, Coventry, UK. Many plants produce ribosome-inactivating proteins (RIPs) — enzymes that act on ribosomes in a highly specific way, thereby inhibiting protein synthesis. Some RIPs can bind to and enter cells, making them among the most toxic substances known. More commonly, however, RIPs are unable to enter healthy cells, and are therefore poorly cytotoxic. Their role in plants is currently a matter of Cited by:

Doctor of Philosophy with a thesis entitled "Diant a ribosome inactivating protein from Dianthus caryophyllus", supervisor Professor l Lord at University of . Chemical contents and medical importance of Dianthus caryophyllus- A review Dianthus caryophyllus var. coronarius L., Dianthus coronarius (L.) .Dianthin 30 and diant were proteins isolated from the leaves of Diathus caryophyllus, were purified by chromatography on CM-cellulose. The molecular weight of dianthin 30 is 29 and Cited by: 4.

Dianthin 30 and 32 from Dianthus caryophyllus: Two inhibitors of plant protein synthesis and their tissue distribution. Archives of Biochemistry and Biophysics , (2), Cited by: greatly from one protein to another, the most active being crotin 2 and crotin 3 from Croton tiglium seeds (Table 1). I a 0. W z 50 U) *_ o P '0 _D _ to q fo L RIPadded (nM) FIG. 1. Effects of dianthin 32 and crotin 3 on E. coli ribosomes: adenine release and protein synthesis inhibition. Adenine released (solid lines) andprotein.


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Dianthin 30, a ribosome inactivating protein from Dianthus caryophyllus L by Giuseppe Antonio Legname Download PDF EPUB FB2

Possesses high antiviral potency, but relatively high toxicity to normal cells in culture and to intact animals. Capable of inhibiting HIV-1 infection and replication (PubMed).Allergy may occcur upon exposure to this protein, which needs to be taken into account when considering it for therapeutic purposes (PubMed).

1 A ribosome inactivating protein from Dianthus caryophyllus L. book. Diant a ribosome inactivating protein from Dianthus caryophyllus L.: cDNA cloning and high level expression in Escherichia coli.

Author: Legname, Giuseppe Antonio. ISNI: Awarding Body: University of Warwick. Diant a ribosome inactivating protein from Dianthus caryophyllus L.: cDNA cloning and high level expression in Escherichia coli. Thesis (Thesis) Find all Author: Legname Ga. The RIP, Dianthin 30 from Dianthus caryophyllus (carnation), was used and expressed in bacterial and insect expression systems.

The bacterial expression experiments were done using the pET expression system in BL21(DE3)pLysS cells. The expression in this system yielded recombinant protein at a very low concentration.

Immunotoxins were prepared with a Ber-H2 (anti-CD30) monoclonal antibody and native or recombinant diant a ribosome-inactivating protein fromDianthus caryophyllus (carnation). Both immunotoxins selectively inhibited protein synthesis by CD30+ cell lines DB (lymphoblastoid, infected with Epstein-Barr virus).

L and L (both from Hodgkin's lymphoma).Cited by:   Dianthin 30 and 32 from Dianthus caryophyllus: two inhibitors of plant protein synthesis and their tissue distribution. Reisbig RR, Bruland O. The ability of dianthin 30 and 32 to inhibit translation in reticulocyte lysates and wheat germ extracts has been studied.

The dianthins, like the A chains of the toxins abrin and ricin, inhibited Cited by: The ability of dianthin 30 and 32 to inhibit translation in reticulocyte lysates and wheat germ extracts has been studied.

The dianthins, like the A chains of the toxins abrin and ricin, inhibited protein synthesis in reticulocyte lysates by inactivating the 60S ribosomal subunit.

They also inhibited, at concentrations of 10 ng/ml, a protein-synthesizing system from wheat germ and inactivated Cited by: Ribosome-inactivating protein dianthin Curated (EC: Search proteins in UniProtKB for this EC number. See the description of this EC number in ENZYME.

The Å structure of dianthin 30 indicates a role of surface potential at the active site of type 1 ribosome inactivating proteins Article in Journal of Structural Biology (2) 1.

Dianthin 30 and diant two proteins isolated from the leaves of Diathus caryophyllus (carnation), were purified to homogeneity by chromatography on CM-cellulose. The of dianthin 30 is 29 and that of dianthin 32 is 31 Both dianthins are glycoproteins containing mannose.

Dianthins inhibit protein synthesis in a lysate of rabbit reticulocytes, with an ID50 Cited by:   Nucleotide sequence of cDNA coding for diant a ribosome inactivating protein from Dianthus protein of ri31, abrin A properties from Dianthus caryophyllus l Cited by: Rabbit antibodies raised against diant a ribosome inactivating protein from carnation (Dianthus caryophyllus) leaves, were used to identify a full length dianthin precursor cDNA clone from a λgt11 expression library.

N-terminal amino acid sequencing of purified dianthin 30 and dianthin 32 confirmed that the clone encoded dianthin Cited by: The DIANTHIN gene encoding a ribosome-inactivating protein (RIP) from Dianthus caryophyllus L. was tested for negative selection in tobacco and rice.

Tobacco leaf discs and scutellum-derived callus of rice were transformed with Agrobacterium tumefaciens strain LBA (pSB1, pJAS1). pJAS1 harbors the DIANTHIN gene under the control of the CaMV 35S by: 9. Dianthins, ribosome-damaging proteins with anti-viral properties from Dianthus caryophyllus L.

(carnation). Stirpe F, Williams DG, Onyon LJ, Legg RF, Stevens WA. Dianthin 30 and diant two proteins isolated from the leaves of Diathus caryophyllus (carnation), were purified to homogeneity by chromatography on CM-cellulose. by: Rabbit antibodies raised against diant a ribosome inactivating protein from carnation (Dianthus caryophyllus) leaves, were used to identify a full length dianthin precursor cDNA clone from.

Dianthin 30 and diant two proteins isolated from the leaves of Diathus caryophyllus (carnation), were purified to homogeneity by chromatography on CM-cellulose.

The of dianthin 30 is 29 and that of dianthin 32 is 31 Both dianthins are glycoproteins containing mannose. They also depurinate extensively DNA and other polynucleotides. The three-dimensional structure of diant a type 1 (single-chain) RIP of Dianthus caryophyllus (leaves), is now described at angstroms, a resolution never achieved before for any RIP.

The fold typical of RIPs is conserved, despite some differences in the loop by: Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety.

Dianthin is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins Cited by: 1. Dianthin 29 was obtained by the final chromatogra- phy step on MONO S HR5/5 as a single protein as judged by SDS-PAGE (Fig.

From comparison to marker proteins its M~ is ca. 29, With reference to the already known RIPs Dianthin 30 and Dianthin 32 from Dianthus caryophyllus L. [18], the name Dianthin. Protein Data Bank file 2AAI. a water molecule of an oxycarbonium ion intermediate, with the conserved residues Arg and Glu being directly involved.

Biosynthesis of ribosome-inactivating proteins Most is known about the biosynthesis of ricin and maize. Tumorous crown gall lines of carnation (Dianthus caryophyllus L.) were obtained by transforming leaf explants by the co-cultivation procedure; transformed lines were checked for their ability to produce in vitro the type 1 ribosome-inactivating proteins dianthins.

Crude extracts from cultured callus were able to inhibit protein synthesis in a cell-free system based on rabbit reticulocyte.as a single-chain RIP for its ribosome-inactivating activity by Irvin and colleagues at the University of Texas, Austin [37–39].

Thus, anti-viral activity became a clue for the discovery of new RIPs, as in the case of dianthin purified from Dianthus caryophyllus ([40], reviewed in [41]).

Starting inCited by: protein dianthin coding mm ribosome inactivating Prior art date Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Abandoned Application number CA Other languages French (fr) Inventor Cited by: 3.