Abstract:
:Two molecular forms of juvenile hormone binding proteins were identified in the larval hemolymph of Bombyx mori by photoaffinity labeling. One form having an Mr of 33 kDa was present constantly in the hemolymph of the third to the fifth instar larvae while the other form having an Mr of 35 kDa was detected in the hemolymph until in the early fifth instar larvae but not in the prewandering larvae and prepupae. A 33 kDa binding protein was purified by hydrophobic interaction chromatography, gel filtration, and native PAGE. Antiserum against 33 kDa binding protein cross-reacted with 35 kDa binding protein on Western blots, suggesting that these binding proteins shared the same epitopes. From the results of saturation binding assays, it was inferred that 33 and 35 kDa binding proteins had a similar binding affinity for JH I. It was revealed that one of these binding proteins, 35 kDa binding protein, was produced in the fat body in a stage-specific manner: fat body of the early fifth instar larvae synthesized both 33 and 35 kDa binding proteins while that of prewandering larvae synthesized only 33 kDa binding protein.
journal_name
Arch Insect Biochem Physioljournal_title
Archives of insect biochemistry and physiologyauthors
Park CH,Kim HRdoi
10.1002/(SICI)1520-6327(1996)33:2<83::AID-ARCH1>3.subject
Has Abstractpub_date
1996-01-01 00:00:00pages
83-98issue
2eissn
0739-4462issn
1520-6327pii
10.1002/(SICI)1520-6327(1996)33:2<83::AID-ARCH1>3.journal_volume
33pub_type
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