Premium
Preparation of toxic radio‐iodinated ricin for use in ricin—ribosome interaction studies
Author(s) -
Lugnier Alain A.J.
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80874-5
Subject(s) - microbiology and biotechnology , physics , ricin , stereochemistry , humanities , chemistry , philosophy , biochemistry , biology , toxin
Radioactive labelling of protein is useful to study interactions and binding of these molecules to cells, membranes as well as to molecular structures. Lactoperoxidase-catalysed iodination of proteins has the advantage of high specific activity and simple methods of preparation. Moreover, the radioactivity is easy to detect. The method of Pages et al. [l] can be wellcontrolled; under mild conditions tyrosyl residues are iodinated but not histidyl residues. Ricin is a highly toxic protein interacting with the 80 S ribosomes [2-51 but its specific target, ribosomal protein or RNA, is not yet known. Radioactive ricin is useful to study this interaction. Inactivation of ricin as a function of the number of iodine atoms incorporated per molecule was studied. Conditions giving an iodinated-ricin of high specific radioactivity without loss of activity were determined.