| Project/Area Number |
10660256
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Zootechnical science/Grassland science
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| Research Institution | Tokyo University of Agriculture & Technology |
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Principal Investigator |
SHIRAI Kunio Scleroprotein and Leather Research Institute, Professor, 農学部, 教授 (70107168)
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| Co-Investigator(Kenkyū-buntansha) |
NOMURA Yoshihiro Scleroprotein and Leather Research Institute, Assistant professor, 農学部, 助手 (10228372)
ISHII Yasuhiro Scleroprotein and Leather Research Institute, Associate professor, 農学部, 助教授 (90015090)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥3,200,000 (Direct Cost: ¥3,200,000)
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| Keywords | hair keratin / solubilized hair keratin / S-sulfokeratein / disulfide form keratin / collagen fibrilogenesis / confibrilogenesis system / collagen / keratin composite / S-スルホン化ケラチン / 共線維形成系 |
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| Research Abstract |
The present research was carried out in 1998 and 1999 to develop a collagen/keratin composite aiming at the utilization of unutilyzed natural resources. 1998 : pig hair was processed into soluble S-sulfokeratein using dithiothreitol (DTT), sulfite and tetrathionate by 60% yield. Characterization of the product was done by SDS-PAGE, amino acid analysis, IR analysis. The product was further fractionated into Bp (microfibril protein) and Bs (matrix protein) and the fractions were characterized by SDS-PAGE and amino acid analysis. The fraction Bs or Bp was further processed into partially reduced S-sulfokeratein by the reaction with DTT. The reaction was monitored by capillary electrophorese. 1999 : The obtained soluble keratein with a different degree of desulfonation was mixed with soluble collagen in the aqueous medium under ice-cooling. The mixture was warmed to set a gel of fibril. The rate of fibrilogenesis and mechanical strength of the gel were determined. The result demonstrated that a 10:1 mixture of collagen and keratin Bs reduced with DTT by a ratio of 1/10 protein produces the strongest gel (twice the control). By similar procedures, a 4:1 mixture of collagen and keratin Bp reduced with 50 times amount of β -mercaptoethanol produced a much stronger mechanical strength of dry film formed by casting than a single species of material collagen or keratin. The present research presented a collagen/keralin composite material having a functionality of SH/SS exchangeability.
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