Journal article
Iodination of peptidyl chloromethyl ketones for protease affinity labels.
- Rauber P Friedrich Miescher-Institut, Basel, Switzerland.
- Wikstrom P
- Shaw E
- 1988-02-01
Published in:
- Analytical biochemistry. - 1988
Affinity Labels
Amino Acid Chloromethyl Ketones
Humans
Iodine
Kallikreins
Protease Inhibitors
Serine Endopeptidases
Thrombin
English
The specificity of peptidyl chloromethyl ketones has been used to label proteases in complex biological systems by incorporating tyrosine into the structure for eventual radioiodination. Contrary to results with iodination of proteins, a mild reagent, that is, one which iodinates at neutrality, was unsuitable, giving complex mixtures with poor reproducibility, apparently because of side reactions at the chloromethyl ketone group. On the other hand, iodine monochloride in acetic acid provided clean products. In the cases examined where a tyrosine residue was not appropriate for the specificity of the target protease, this residue was located well displaced from the primary specificity site. The resultant diiodotyrosine-containing derivatives were generally highly active as protease inhibitors. The p-aminobenzoyl group was used as an alternative to tyrosine as an iodinatable component.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1016/0003-2697(88)90316-8
- PMID 3163239
- Persistent URL
- https://sonar.ch/global/documents/100868
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