Isolation and characterization of a high molecular weight JH-III transport protein in the hemolymph of locusta migratoria

✍ Scribed by A. B. Koopmanschap; C. A. D. De Kort

• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 907 KB
• Volume: 7
• Category: Article
• ISSN: 0739-4462
• DOI: 10.1002/arch.940070204

✦ Synopsis

The juvenile hormone binding protein in Locusta migratoria i s a very high density lipoprotein of M, = 566,000. It contains 15% lipid and i s composed of six seemingly identical subunits of M, = 77,000. It is a minor protein, constituting I-2% of the total hemolymph proteins. Its concentration fluctuates with total protein content and follows a cyclic pattern related to the molting cycles.

The binding protein has a high affinity for (IOR)-juvenile hormone 111. The dissociation constant for the hormone is 3.7 f 0.6 nM, and one binding molecule contains six hormone-specific binding sites. The concentration of binding sites in the hemolymph i s therefore very high, reaching a value of 26 pM in the last larval instar and 11 pM in the adult male.