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  • Title: Labelling of the human erythrocyte glucose transporter with 3H-labelled cytochalasin B occurs via protein photoactivation.
    Author: Deziel M, Pegg W, Mack E, Rothstein A, Klip A.
    Journal: Biochim Biophys Acta; 1984 May 30; 772(3):403-6. PubMed ID: 6539126.
    Abstract:
    Irradiation of human erythrocyte membranes with 3H-labelled cytochalasin B results in specific photolabelling of the glucose transporter. The action spectrum of photolabelling has a maximum at approx. 280 nm, whereas the absorption spectrum of cytochalasin B is maximal at 210 nm. By irradiating with narrow-band-width light centered at 280 nm for 2 h, 8% of the transporters become covalently labelled and 47% of the remaining cytochalasin B-binding sites are obliterated. We conclude that photolabelling driven by narrow-bandwidth irradiation proceeds via photoactivation of an aromatic amino acid residue on the transporter molecule, and when compared to wide-bandwidth irradiation, permits more efficient incorporation of the label without causing additional photodamage to the remaining transporters.
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