title: Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L.
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.
authors.affiliation: Dipartimento di Chimica organica e biologica, Università di Napoli, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Parente
authors.forename: P
authors.initials: P
authors.lastname: De Luca
authors.forename: A
authors.initials: A
authors.lastname: Bolognesi
authors.forename: L
authors.initials: L
authors.lastname: Barbieri
authors.forename: M G
authors.initials: MG
authors.lastname: Battelli
authors.forename: A
authors.initials: A
authors.lastname: Abbondanza
authors.forename: M J
authors.initials: MJ
authors.lastname: Sande
authors.forename: G S
authors.initials: GS
authors.lastname: Gigliano
authors.forename: P L
authors.initials: PL
authors.lastname: Tazzari
authors.forename: F
authors.initials: F
authors.lastname: Stirpe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line / Q000187:drug effects; D005260:Female; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000633:toxicity; D000922:Immunotoxins / Q000302:isolation & purification*; D051379:Mice; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000633:toxicity; D014176:Protein Biosynthesis; D011817:Rabbits; D051381:Rats; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D000076985:Saporins; D012639:Seeds / Q000737:chemistry*
chemical_list: D000922:Immunotoxins; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D006026:Glycoside Hydrolases; D009699:N-Glycosyl Hydrolases; D000076985:Saporins