Synthesis of juvenile hormone binding proteins by the fat body of Manduca sexta
Autor: | J. Nowock, Lawrence I. Gilbert, W. E. Bollenbacher, Walter Goodman |
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Rok vydání: | 1975 |
Předmět: |
Immunodiffusion
animal structures Immunoprecipitation Plasma protein binding Immunoelectrophoresis Salivary Glands Endocrinology Hemolymph medicine Animals Cells Cultured Gel electrophoresis biology medicine.diagnostic_test Binding protein Muscles fungi biology.organism_classification Precipitin Tests Juvenile Hormones Lepidoptera Biochemistry Adipose Tissue Manduca sexta Organ Specificity Larva Animal Science and Zoology Carrier Proteins Lipoprotein Protein Binding |
Zdroj: | General and comparative endocrinology. 27(2) |
ISSN: | 0016-6480 |
Popis: | The hemolymph of fourth instar Manduca sexta larvae contains both a relatively low molecular weight protein and a large molecular weight lipoprotein that are capable of binding the C18 juvenile hormone (JH). The low molecular weight binding protein (BP) has a much greater affinity for JH than the lipoprotein. A variety of organs were incubated in vitro and both the media and homogenate supernatants were analyzed in order to determine the site of synthesis of the BP. By obtaining antibodies against the BP, immunoprecipitation and immunoelectrophoretic studies could be conducted along with polyacrylamide slab gel electrophoresis and double labeling experiments. The data strongly suggest that the fat body is the insect's source of JH-BP and that the BP is rapidly released from the fat body. That is, the fat body synthesizes BP but does not store it in significant quantities. The same appears to be true of the specific lipoprotein capable of binding JH. |
Databáze: | OpenAIRE |
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