Transglutaminase amine substrates for photochemical labeling and cleavable cross-linking of proteins
A new procedure for the photochemical labeling of peptides and for the production of cleavable cross-links between protein molecules is given. This method is mediated through the catalytic action of the enzyme guinea pig liver transglutaminase. Each of the labeling and cross-linking reagents describ...
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Veröffentlicht in: | The Journal of biological chemistry 1980-02, Vol.255 (3), p.1175-1180 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A new procedure for the photochemical labeling of peptides and for the production of cleavable cross-links between protein
molecules is given. This method is mediated through the catalytic action of the enzyme guinea pig liver transglutaminase.
Each of the labeling and cross-linking reagents described here is an amine substrate for transglutaminases and, because of
the narrow specificity of these enzymes, is introduced covalently only at the gamma-carboxamide group of available peptide-bound
glutamine residues. Cross-linking results either solely through the action of the enzyme in the case of a diamine substrate,
or by subsequent photolysis in the case of photosensitive amine substrates. Cleavable bonds in several of the substrates are
disulfide or vicinal hydroxyl groups. The validity of the procedure is demonstrated by the preparation of photosensitive derivatives
of substance P and glucagon 1-6 and in the cleavable covalent cross-linking of guanidinated beta-casein. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)86159-8 |