Suberimidate crosslinking shows that a rod-shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains
- 15 October 1978
- journal article
- Published by Wiley in FEBS Letters
- Vol. 94 (2) , 365-367
- https://doi.org/10.1016/0014-5793(78)80978-8
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
- Chemical Cross-Linking: Reagents and Problems in Studies of Membrane StructureAnnual Review of Biochemistry, 1977
- Crosslinking and Self-Crosslinking in Keratin FibersPublished by Springer Nature ,1977
- Three-chain merokeratin from wool may be a fragment of the microfibril component macromoleculeNature, 1977
- Structure of the α-keratin microfibrilJournal of Molecular Biology, 1976
- Self-assembly of bovine epidermal keratin filaments in vitroJournal of Molecular Biology, 1976
- Proteins and Sodium Dodecyl Sulfate: Molecular Weight Determination on Polyacrylamide Gels and Related ProceduresPublished by Elsevier ,1975
- Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric ProteinsProceedings of the National Academy of Sciences, 1970