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Histochemical detection of binding sites for human growth hormone using biotinylated ligand

J Bentham, R Aplin and MR Norman

Department of Clinical Biochemistry, King's College Hospital, London, United Kingdom.

Recombinant human growth hormone was covalently linked to biotin via a six-carbon spacer arm. Biotinylation was confirmed by electrophoresis and mass spectrometry showed that approximately 50% of the hormone was monobiotinylated. The modified growth hormone (GH) was shown to bind to the GH receptor of IM9 human lymphoid cells with an affinity of 0.55 x 10(9) M-1. Bioactivity of biotinylated GH measured in the Nb2 bioassay was 53.9% that of unlabeled GH. GH binding sites on human IM9 cells were visualized histochemically with the biotinylated hormone, a technique that provides a means of identifying receptors for GH on target cells in vitro.

Volume 42, Issue 1, pp. 103-107, 01/01/1994
Copyright © 1994 by The Histochemical Society


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