DOI: 10.1002/app.1993.070471107. Cross‐linking structure of keratin. IV. The number of cross‐linkages in low‐sulfur components and the volume fraction of high‐sulfur domains in various α‐keratin fibers

Cross‐linking structure of keratin. IV. The number of cross‐linkages in low‐sulfur components and the volume fraction of high‐sulfur domains in various α‐keratin fibers

10.1002/app.1993.070471107

Crossref journal-article

Wiley

Journal of Applied Polymer Science (311)

Abstract

AbstractVarious α‐keratin fibers that had been treated with an 11M LiBr solution containing N‐ethylmaleimide showed typical rubberlike elasticity in a solution composed of equal volumes of 8M LiBr and diethylene glycol mono‐n‐butyl ether. Stress—strain relations of the swollen fibers were treated with a two‐phase model: a mechanically stable phase of higher cross‐linked domains and a rubber phase with lower cross‐link density. Stress—strain curves for a variety of keratins (three different human hairs, six different wools, mohair, cashmere, llama, alpaca, angora, and opossum) were analyzed by applying non‐Gaussian chain statistics to the swollen keratin network, including microdomains, which act as reinforcing filler particles in rubber. The phase structures of unswollen domains and swollen rubber were considered to originate from different structural components characteristic of α‐keratin, namely, the high‐sulfur matrix and the low‐sulfur microfibrils being randomized by swelling. It has been suggested that (1) the modulus of swollen fibers increases with increase of the content of disulfide (SS) in keratins, (2) the volume fraction of high‐sulfur domains increases with increase of SS content, and (3) the number of intermolecular cross‐links in the rubber region of low‐sulfur proteins is virtually the same among keratins and reaches about 65–75% of the SS linkages in the corresponding proteins. Some discussion has been made on the SS bonding in situ, namely, SS linkages between the low‐sulfur proteins, between the low‐sulfur and the high‐sulfur proteins, and between the high‐sulfur proteins in keratins. © 1993 John Wiley & Sons, Inc.

Bibliography

Arai, K., Hirata, T., Nishimura, S., Hirano, M., & Naito, S. (1993). Crossâlinking structure of keratin. IV. The number of crossâlinkages in lowâsulfur components and the volume fraction of highâsulfur domains in various Î±âkeratin fibers. Journal of Applied Polymer Science, 47(11), 1973â1981. Portico.

Authors 5

Kozo Arai (first)
Taishi Hirata (additional)
Shushi Nishimura (additional)
Mitsushige Hirano (additional)
Sachio Naito (additional)

References 47 Referenced 9

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{'key': 'e_1_2_1_10_2', 'first-page': '495', 'volume-title': 'The Biology of Wool and Hair', 'author': 'Zahn H.', 'year': '1989'} / The Biology of Wool and Hair by Zahn H. (1989)
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{'key': 'e_1_2_1_36_2', 'first-page': '149', 'volume': '2', 'author': 'Crewther W. G.', 'year': '1964', 'journal-title': 'J. Polym. Sci.'} / J. Polym. Sci. by Crewther W. G. (1964)
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Dates

Type	When
Created	22 years, 4 months ago (April 15, 2003, 4:58 p.m.)
Deposited	1 year, 9 months ago (Nov. 20, 2023, 3:31 p.m.)
Indexed	3 months ago (May 27, 2025, 4:29 a.m.)
Issued	32 years, 5 months ago (March 15, 1993)
Published	32 years, 5 months ago (March 15, 1993)
Published Online	22 years, 5 months ago (March 10, 2003)
Published Print	32 years, 5 months ago (March 15, 1993)

Funders 0

None

BibTeX

@article{Arai_1993, title={Cross‐linking structure of keratin. IV. The number of cross‐linkages in low‐sulfur components and the volume fraction of high‐sulfur domains in various α‐keratin fibers}, volume={47}, ISSN={1097-4628}, url={http://dx.doi.org/10.1002/app.1993.070471107}, DOI={10.1002/app.1993.070471107}, number={11}, journal={Journal of Applied Polymer Science}, publisher={Wiley}, author={Arai, Kozo and Hirata, Taishi and Nishimura, Shushi and Hirano, Mitsushige and Naito, Sachio}, year={1993}, month=mar, pages={1973–1981} }

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