A ribosome-inactivating protein similar to those already known (Stirpe and Barbieri (1986) FEBS Lett. 195, 1-8) was purified from the seeds of Momordica cochinchinensis. This protein, for which the name of momorcochin-S is proposed, is a glycoprotein, has an Mr of approx. 30,000, and an alkaline isoelectric point and can be considered as an iso-form of the previously purified momorcochin from the roots of M. cochinchinensis. Momorcochin-S inhibits protein synthesis by a rabbit-reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and alters rRNA in a similar manner as the A-chain of ricin and related toxins (Endo et al. (1987) J. Biol. Chem. 262, 5908-5912). Momorcochin-S was linked to a monoclonal antibody (8A) against human plasma cells, and the resulting immunotoxin was selectively toxic to target cells.

Purification and properties of a new ribosome-inactivation protein with RNA N-glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis / Bolognesi A.; Barbieri L.; Carnicelli D.; Abbondanza A.; Cenini P.; Falasca A.I.; Dinota A.; Stirpe F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS. - ISSN 0304-4165. - STAMPA. - 993:2-3(1989), pp. 287-292. [10.1016/0304-4165(89)90178-5]

Purification and properties of a new ribosome-inactivation protein with RNA N-glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis

Bolognesi A.;Barbieri L.;Carnicelli D.;Abbondanza A.;Cenini P.;Stirpe F.
1989

Abstract

A ribosome-inactivating protein similar to those already known (Stirpe and Barbieri (1986) FEBS Lett. 195, 1-8) was purified from the seeds of Momordica cochinchinensis. This protein, for which the name of momorcochin-S is proposed, is a glycoprotein, has an Mr of approx. 30,000, and an alkaline isoelectric point and can be considered as an iso-form of the previously purified momorcochin from the roots of M. cochinchinensis. Momorcochin-S inhibits protein synthesis by a rabbit-reticulocyte lysate and phenylalanine polymerization by isolated ribosomes, and alters rRNA in a similar manner as the A-chain of ricin and related toxins (Endo et al. (1987) J. Biol. Chem. 262, 5908-5912). Momorcochin-S was linked to a monoclonal antibody (8A) against human plasma cells, and the resulting immunotoxin was selectively toxic to target cells.
1989
Purification and properties of a new ribosome-inactivation protein with RNA N-glycosidase activity suitable for immunotoxin preparation from the seeds of Momordica cochinchinensis / Bolognesi A.; Barbieri L.; Carnicelli D.; Abbondanza A.; Cenini P.; Falasca A.I.; Dinota A.; Stirpe F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS. - ISSN 0304-4165. - STAMPA. - 993:2-3(1989), pp. 287-292. [10.1016/0304-4165(89)90178-5]
Bolognesi A.; Barbieri L.; Carnicelli D.; Abbondanza A.; Cenini P.; Falasca A.I.; Dinota A.; Stirpe F.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/959192
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