Three ribosome-inactivating proteins (RIPs) similar to those already known (Stirpe et al. (1992) Bio/Technology 10, 405-412) were purified from the seeds of Phytolacca dioica. These proteins, called Phytolacca dioica RIPs (PD-S1, PD-S2 and PD-S3 RIPs), are glycoproteins, with M(r) approx. 30,000, inhibit protein synthesis by a rabbit reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and depurinate rat liver rRNA in an apparently identical manner as the A-chain of ricin and other RIPs (Endo et al. (1987) J. Biol. Chem. 262, 5908-5912). Part of the purified rat liver ribosomes appeared resistant to the action of PD-S RIPs. The most abundant protein, PD-S2 RIP, gave a weak or nil cross-reaction with sera against various other RIPs, including a pokeweed antiviral protein from the roots of Phytolacca americana. PD-S2 RIP was linked to a monoclonal antibody (Ber-H2) against the CD30 human lymphocyte antigen and the resulting immunotoxin was selectively toxic to the CD30 + Hodgkin's lymphoma-derived L540 cell line.

Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L / Parente A.; De Luca P.; Bolognesi A.; Barbieri L.; Battelli M.G.; Abbondanza A.; Sande M.J.W.; Gigliano G.S.; Tazzari P.L.; Stirpe F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA, N. GENE STRUCTURE AND EXPRESSION. - ISSN 0167-4781. - STAMPA. - 1216:1(1993), pp. 43-49. [10.1016/0167-4781(93)90035-C]

Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L

Parente A.;De Luca P.;Bolognesi A.;Barbieri L.;Battelli M. G.;Abbondanza A.;Stirpe F.
1993

Abstract

Three ribosome-inactivating proteins (RIPs) similar to those already known (Stirpe et al. (1992) Bio/Technology 10, 405-412) were purified from the seeds of Phytolacca dioica. These proteins, called Phytolacca dioica RIPs (PD-S1, PD-S2 and PD-S3 RIPs), are glycoproteins, with M(r) approx. 30,000, inhibit protein synthesis by a rabbit reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and depurinate rat liver rRNA in an apparently identical manner as the A-chain of ricin and other RIPs (Endo et al. (1987) J. Biol. Chem. 262, 5908-5912). Part of the purified rat liver ribosomes appeared resistant to the action of PD-S RIPs. The most abundant protein, PD-S2 RIP, gave a weak or nil cross-reaction with sera against various other RIPs, including a pokeweed antiviral protein from the roots of Phytolacca americana. PD-S2 RIP was linked to a monoclonal antibody (Ber-H2) against the CD30 human lymphocyte antigen and the resulting immunotoxin was selectively toxic to the CD30 + Hodgkin's lymphoma-derived L540 cell line.
1993
Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L / Parente A.; De Luca P.; Bolognesi A.; Barbieri L.; Battelli M.G.; Abbondanza A.; Sande M.J.W.; Gigliano G.S.; Tazzari P.L.; Stirpe F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA, N. GENE STRUCTURE AND EXPRESSION. - ISSN 0167-4781. - STAMPA. - 1216:1(1993), pp. 43-49. [10.1016/0167-4781(93)90035-C]
Parente A.; De Luca P.; Bolognesi A.; Barbieri L.; Battelli M.G.; Abbondanza A.; Sande M.J.W.; Gigliano G.S.; Tazzari P.L.; Stirpe F.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/959148
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