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| Content Provider | PubMed Central |
|---|---|
| Author | Chang, Ernest S. Coudron, Thomas A. Bruce, Marilyn J. Sage, Becky A. O'connor, John D. Law, John H. |
| Abstract | Insect cells of an established line, Drosophila Kc cells, take up and metabolize juvenile hormone (JH). The cytoplasm of these cells contains a protein that binds JH with specificity, saturability, and high affinity (K d = 1.56 × 10-8 M). The kinetics for the specific binding and dissociation of JH I were independently measured, and the rate constants were found to be k a = 1.3 × 106 M-1 min-1, k d = 1.3 × 10-2 min-1, respectively. All three juvenile hormones bind to the protein with comparable affinities; the corresponding acid or diol metabolites of JH I are not bound. About 2500 hormone-binding protein molecules are present per cell. The protein has a molecular weight of 80,000 as estimated by gel permeation chromatography and by sucrose gradient sedimentation. The properties of this protein suggest that it functions as a cytoplasmic receptor for juvenile hormone. |
| Starting Page | 4657 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 8 |
| Volume Number | 77 |
| Language | English |
| Publisher Date | 1980-08-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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