| Literature DB >> 2327576 |
M Joniau1, K Coudijzer, M De Cuyper.
Abstract
We have studied the capacity of different iodinated derivatives of phenylalanine and tyrosine to inhibit the incorporation of [3H]tyrosine into tubulin catalyzed by tubulin:tyrosine ligase. In contrast to thyronine and its iodinated derivatives, iodotyrosines were efficient inhibitors. That they also functioned as substrates of the enzyme was shown by the effective incorporation of [125I]mono- and diiodotyrosine into tubulin. The label was shown to be located at the carboxy terminus. Labeling by this method conserves the polymerization capacity of tubulin in contrast with classical radioiodination methods involving oxidation.Entities:
Mesh:
Substances:
Year: 1990 PMID: 2327576 DOI: 10.1016/0003-2697(90)90689-7
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365