Bacterial Proteaseにより分離されたミオシン尾部の熱安定性に関する研究

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タイトル別名
  • The Study on the Thermostability of Myosin Rod Isolated by a Bacterial Protease
  • Bacterial Protease ニ ヨリ ブンリサレタ ミオシン ビブ

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This study was undertaken to obtain more information on the thermostability of light meromyosin, the tail portion of myosin molecule which determines the solubility of parent molecule. The rod portion of myosin (LMM-BPNP) was obtained by cleaving rabbit skeletal muscle myosin with a neutral protease of Bacillus polymixa (BPNP). Some physico-chemical properties of LMM-BPNP were studied following the changes in its mass and partial structure before and after heat treatment, through ultraviolet difference spectrum and solubility. In a previous paper7), we have already shown that the changes in measurements of ORD, CD and viscosity of LMM-BPNP are almost completely reversible, since stepwise cooling (70-20°C) of the fully denatured protein yields helix contents identical with those obtained during the heating process (20-70°C). The changes in -ΔA285 of LMM-BPNP, however, did not show complete reversibility by cooling. On the other hand, like LMM Fr 1 (tryptic digested myosin rod portion) LMM-BPNP became soluble at low inoic strength (I_??_0.1) after heat treatment. At higher ionic strengths, LMM-BPNP showed the solubility similar to that of LMM-C (CNBr cleaved myosin rod portion). The molecular weight of 135, 000-150, 000 for LMM-BPNP without heat treatment was calculated from the data of intrinsic viscosity in 6M guanidine-HCl. The present findings, thus, show that LMM-BPNP possesses properties intermidiate to those of LMM Fr 1 and LMM-C.

収録刊行物

  • 日本畜産学会報

    日本畜産学会報 47 (3), 147-152, 1976

    公益社団法人 日本畜産学会

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