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Fluorescent labeling of hormone receptors in viable cells preparation and properties of highly fluorescent derivatives of epidermal growth factor and insulin



Fluorescent labeling of hormone receptors in viable cells preparation and properties of highly fluorescent derivatives of epidermal growth factor and insulin



Proceedings of the National Academy of Sciences of the United States of America 75(5): 2135-2139



Highly fluorescent analogs in insulin and [mouse submaxillary gland] epidermal growth factor [EGF] were prepared by the covalent attachment of these peptides to .alpha.-lactalbumin molecules that were highly substituted (i.e., 7 to 1) with rhodamine molecules. The .alpha.-lactalbumin was specifically linked to the lysine residue of insulin or to the .alpha.-amino group of EGF. The insulin derivative retained 1.15% of its potency in stimulating glucose oxidation in fat cells but retained about 8.3% of its binding affinity toward receptors. The EGF derivative was completely active in binding to fibroblast receptors and 40% as potent as the native hormone in stimulating DNA synthesis. These highly fluorescent derivatives were suitable for the specific visual labeling of receptor sites in viable cells and for measuring the lateral mobilities of the receptor-hormone complexes by fluorescent photobleaching recovery techniques. By these methods it was shown that the hormone-receptor complexes can move laterally in the plane of the plasma membrane with a diffusion coefficient of (3-5) .times. 10-10 cm2/s.

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Accession: 005472115

Download citation: RISBibTeXText

PMID: 209452

DOI: 10.2307/68399


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