Sanshi-Konchu Biotec
Online ISSN : 1884-7943
Print ISSN : 1881-0551
ISSN-L : 1881-0551
Volume 75 , Issue 2
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  • Yoko Takasu, Hiromi Yamada, Kozo Tsubouchi
    2006 Volume 75 Issue 2 Pages 133-139
    Published: 2006
    Released: August 01, 2007
    JOURNALS FREE ACCESS
    Among the three main components of cocoon sericin of the silkworm Bombyx mori, sericin A, the sericin secreted at the anterior portion of the middle silk gland, showed a different property compared to the two other components. After wetting the cocoon, sericin M and P decreased their solubility in hot water, and the decrease was enhanced by heat. On the other hand, sericin A apparently did not decrease its solubility after wetting and was extracted from cocoons even after being steamed. The FT-IR spectra of purified sericin films showed that sericin M could form a higher content of β-sheet structure than sericin A. These results indicate that the decrease in solubility of sericins M and P is due to β-sheet formation, which was considered to result from the serine-rich sequence composed of multiple 38-amino acid repeats.
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