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• W1972620480 abstract "The 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 bond." @default.
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• W1972620480 date "1999-06-01" @default.
• W1972620480 modified "2023-10-16" @default.
• W1972620480 title "Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori" @default.
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• W1972620480 doi "https://doi.org/10.1016/s0167-4838(99)00088-6" @default.
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