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Chromatographic isolation of α-glucosidases from the taste hair rich tarsi of the flyProtophormia terraenovae. Their possible role as sugar receptor proteins

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Summary

Extracts of the taste hair rich tarsi of the pro- and mesothoracic legs of the flyProtophormia terraenovae contain five chromatographically separable α-glucosidases (E.C. 3.2.1.20). These glucosidases were characterized according to their substrate specificities, their Michaelis constants and their pH optima. The enzymes GLU I, III and V show a broad specificity for several α-glucosides (sucrose, maltose, turanose, palatinose, melezitose and p-nitrophenyl-α-glucoside). The GLU II and IV split sucrose especially with extraordinarily high Michaelis constants (0.1–0.2 M). The properties of the fly enzymes were compared with those of other origine (intestine of mammals, yeast), but especially with those of the fly's taste hair rich labella (Morita and coworkers, 1972–1974). The enzyme GLU III exhibits properties indicating that it may be the sugar receptor protein in question.

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Authors and Affiliations

  1. Zoologisches Institut der Universität Heidelberg, Heidelberg, Germany

    J. Kühner

  2. Fachbereich Biologie der Universität Regensburg, Regensburg, Germany

    K. Hansen

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  1. J. Kühner
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  2. K. Hansen
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Supported by the Schwerpunktprogramm Rezeptorphysiologie der Deutschen Forschungsgemeinschaft.

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Kühner, J., Hansen, K. Chromatographic isolation of α-glucosidases from the taste hair rich tarsi of the flyProtophormia terraenovae. Their possible role as sugar receptor proteins. J. Comp. Physiol. 99, 257–270 (1975). https://doi.org/10.1007/BF00613839

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