Juvenile Hormone Binding Protein and Transferrin from Galleria mellonella Share a Similar Structural Motif
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Abstract
It has been previously suggested that juvenile hormone binding protein(s) (JHBP) belongs to a new class of proteins. In the search for other protein(s) that may contain structural motifs similar to those found in JHBP, hemolymph from Galleria mellonella (Lepidoptera) was chromatographed over a Sephadex G 200 column and resulting fractions were subjected to SDSPAGE, transferred onto nitrocellulose membrane and scanned with a monoclonal antibody, mAb 104, against hemolymph JHBP. Two proteins yielded a positive reaction with mAb 104, one corresponding to JHBP and the second corresponding to a transferrin, as judged from Nterminal amino acid sequencing (KPNYKIXVPQKFLKEXEQMLEVXT) and Ferene S staining. Transferrin was purified to about 80% homogeneity using a twostep procedure including Sephadex G-200 gel filtration and HPLC MonoQ column chromatography. Panning of a random peptide display library and analysis with immobilized synthetic peptides were applied for finding a common epitope present in JHBP and the transferrin molecule. The postulated epitope motif recognized by mAb 104 in the JHBP sequence is RDTKAVN, and is localized at position 82 88.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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