The DOI matches its Crossref record; 39 of the 40 references it cites were found in a registry or an index.
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
Open accessAbstract
Silk fibroin produced by the silkworm Bombyx mori consists of a heavy chain, a light chain, and a glycoprotein, P25. The heavy and light chains are linked by a disulfide bond, and P25 associates with disulfide-linked heavy and light chains by noncovalent interactions. Quantitative enzyme-linked immunosorbent assay revealed that molar ratios of the heavy chain, light chain, and P25 were 6:6:1, both in cocoons and in fibroin secreted into the lumen of posterior silk gland. Trace amounts of fibroin produced by three "naked pupa" mutants of B. mori lacked the light chain, but the molar ratio of heavy chain and P25 was also 6:1. Gel filtration chromatography and sedimentation equilibrium analysis demonstrated that a large protein complex of approximately 2.3 MDa, designated an elementary unit of fibroin having 6:6:1 molar ratios of the heavy chain, light chain, and P25, existed in posterior silk gland cells. Inaccessibility of biotinylated concanavalin A to the native elementary unit and partial dissociation of the elementary unit after incubation with excess N-glycosidase F or endoglycosidase H suggest that a single molecule of P25 is located internally and plays an important role in maintaining integrity of the complex.
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“At present, it is generally believed that silk fibroin is mainly composed of H chain, L chain, and P25 glycoprotein, with the molecular ratio of H:L:P25 = 6:6:1 [21].”
From Recent Advances in Silk Fibroin-Based Composites for Bone Repair Applications: A Review (2025) · cites this paper as [21]
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Silk fibroin biomaterials for tissue regenerations
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Metadata
- Authors
- Inoue, S., Tanaka, K., Arisaka, F., Kimura, S., Ohtomo, K., & Mizuno, S.
- Affiliations
- Tohoku University (JP)
- Tokyo Institute of Technology (JP)
- Chiba University (JP)
- Corresponding author
- Mizuno, Shigeki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 275
- Issue
- 51
- Pages
- 40517-40528
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2120240537
- Cited by
- 784
- References
- 40
- Citations by year
- 2026: 46 · 2025: 49 · 2024: 69 · 2023: 43 · 2022: 57 · 2021: 53 · 2020: 62 · 2019: 39 · 2018: 36 · 2017: 28 · 2016: 32 · 2015: 45 · 2014: 41 · 2013: 25 · 2012: 24
- FWCI
- 3.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Silkworms and Sericulture Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- silk fibroin, Bombyx mori, heavy chain, light chain, molar ratio, posterior silk gland, disulfide bonds, non-covalent interactions, protein complexes, N-glycosidase F, endoglycosidase H, concanavalin A, glycosylation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Disulfides, DNA, Electrophoresis, Polyacrylamide Gel, Fibroins, Glycoproteins, Molecular Sequence Data, Molecular Weight, Oligosaccharides, Protein Conformation, Bombyx, Insect Proteins, Silk
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