Biochemical studies on ricin. XXVI. Primary structure of Ala chain of ricin D.
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چکیده
منابع مشابه
Kinetic analysis of choriocarcinoma cell intoxication induced by ricin and ricin A chain immunotoxin.
The kinetics of protein synthesis inhibition was studied in the choriocarcinoma-derived BeWo cell line treated with ricin and an immunotoxin (IT) constructed by linking a specific antibody to the A chain of ricin. The IT was specifically cytotoxic to BeWo and other choriocarcinoma cells. The multistep process underlying this kinetics was explored using two mathematical models where the protein ...
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Intracellular activation of ricin and of the ricin A-chain (RTA) immunotoxins requires reduction of their intersubunit disulfide(s). This crucial event is likely to be catalyzed by disulfide oxidoreductases and precedes dislocation of the toxic subunit to the cytosol. We investigated the role of protein disulfide isomerase (EC 5.3.4.1, PDI), thioredoxin (Trx), and thioredoxin reductase (EC 1.8....
متن کاملStructure-based identification of a ricin inhibitor.
Ricin is a potent cytotoxin which has been used widely in the construction of therapeutic agents such as immunotoxins. Recently it has been used by governments and underground groups as a poison. There is interest in identifying and designing effective inhibitors of the ricin A chain (RTA). In this study computer-assisted searches indicated that pterins might bind in the RTA active site which n...
متن کاملStructure-Based Design of Ricin Inhibitors
Ricin is a potent cytotoxin easily purified in large quantities. It presents a significant public health concern due to its potential use as a bioterrorism agent. For this reason, extensive efforts have been underway to develop antidotes against this deadly poison. The catalytic A subunit of the heterodimeric toxin has been biochemically and structurally well characterized, and is an attractive...
متن کاملRNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes.
The modification reaction of 28 S rRNA in eukaryotic ribosomes by ricin A-chain was characterized. To examine whether ricin A-chain release any bases from 28 S rRNA, rat liver ribosomes were incubated with a catalytic amount of the toxin, and a fraction containing free bases and nucleosides was prepared from the postribosomal fraction of the reaction mixture by means of ion-exchange column chro...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1979
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.43.2221