The haemolymph of the adult Colorado potato beetle, Lepinotarsa decemlineata Say, contains a high molecular weight (MW > 200,000) JH-III specific binding protein. The Kd value of the protein for racemic JH-III is 1.3 ± 0.2 × 10−7 M. It has a lower affinity for racemic JH-I and it does not bind JH-III-diol or JH-III-acid. The binding protein does discriminate between the enantiomers of synthetic, racemic JH-III as was determined by stereochemical anaysis of the bound and the free JH-III. Incubation of racemic JH-III with crude haemolymph results in preferential formation of (10S)-JH-III-acid, the unnatural configuration. The JH-esterase present in L. decemlineata haemolymph is not enantioselective. It is concluded that the most important function of the binding protein is that of a specific carrier, protecting the natural hormone against degradation by esterases. The carrier does not protect JH-I as efficiently as the lower homologue.
| Identifer | oai:union.ndltd.org:Potsdam/oai:kobv.de-opus-ubp:1677 |
| Date | January 1983 |
| Creators | Kort, C. A. D. de, Peter, Martin G., Koopmanschap, A. B. |
| Publisher | Universität Potsdam, Mathematisch-Naturwissenschaftliche Fakultät. Institut für Chemie, Extern. Extern |
| Source Sets | Potsdam University |
| Language | English |
| Detected Language | English |
| Type | Postprint |
| Format | application/pdf |
| Source | Insect Biochemistry. - 13 (1983), 5, pp. 481 - 487. ISSN 0020-1790 |
| Rights | http://opus.kobv.de/ubp/doku/urheberrecht.php |
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