Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages
Author:
Affiliation:
1. State Key Laboratory of Silkworm Genome Biology, Southwest University, 216, Tiansheng Road, Beibei, Chongqing 400716, China
Publisher
American Chemical Society (ACS)
Subject
General Chemistry,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/pr4005772
Reference66 articles.
1. Polypeptides of fibroin and sericin secreted from the different sections of the silk gland in Bombyx mori
2. Immunological Identification of the Major Disulfide-Linked Light Component of Silk Fibroin1
3. Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the H-L complex of silk fibroin produced by Bombyx mori
4. Silk Fibroin of Bombyx mori Is Secreted, Assembling a High Molecular Mass Elementary Unit Consisting of H-chain, L-chain, and P25, with a 6:6:1 Molar Ratio
5. Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori
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