Unfolding manner of walleye pollack light meromyosin upon heating

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Heat-induced unfolding manner of light meromyosin (LMM) prepared from walleye pollack Theragra chalcogramma was investigated by circular dichroism spectrometry and α-chymotryptic digestion. α-Helix content of the LMM was originally 88% at 5°C, but decreased to 15% by increasing the temperature to 50°C. α-Chymotryptic digestion of the LMM and subsequent amino acid sequencing of the digests showed that unfolding of the LMM initiated in C-terminal region and progressed toward N-terminal region. When the LMM was digested with α-chymotrypsin after heat-treated at 50°C for 5min, the 42-kDa fragment corresponding to N-terminal approximately 2/3 region of the LMM and many smaller peptide fragments derived from remaining C-terminal 1/3 region were produced. These results indicate that the N-terminal 2/3 and C-terminal 1/3 regions of the LMM reversibly and irreversibly unfolding regions, respectively, upon heating.

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