PubMed:10366732
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10366732","sourcedb":"PubMed","sourceid":"10366732","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10366732","text":"Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori.\nThe analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide 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