Structure of Muramidase (Lysozyme):V. Effect of N, N-Dimethylformamide and the Role of Disulfide Bonds in the Stability of Muramidase

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  • HAMAGUCHI KOZO
    the Division of Physical Chemistry, Institute for Prothein Research, Osaka University

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In order to clarify the role of disulfide bonds in the muramidase molecule, optical rotatory and ultraviolet spectral properties of muramidase have been studied in DMF-water mixtures with and without mercaptoethanol.<br> Without mercaptoethanol, the decreases in both the values of-a0 and-b0 occur above 35% DMF. However, the decrease in the value of-a0 became more significant above 70% DMF. On the other hand, denaturation blue shifts appear above 60% DMF. This fact suggests that the β-structure appears after the disruption of the hydrophob;, c region of the muramidase molecule has occured.<br> In the presence of mercaptoethanol, the value of b0 is constant up to 45% DMF, while difference spectra show large denaturation blue shifts when compared the spectrum in DMF-water mixtures containing mercaptoethanol with that in the same solvent without mer-captoethanol in the concentration range be-tween 30 and 50% DMF. This fact suggests that some of the disulfide bonds in the mura-midase molecule plays a role for stabilizin Lydrgphobic region and not helicall part.<br> The decreases in both the values of-a0 and-b0 occur in DMF-water mixtures above 45% DMF containing mercaptoethanol. This may be due to the formation of β-structure.<br> The author is grateful to Prof. T. Isemura for his interest in this work. Thanks are also due to Dr. T. Takagi for his discussions and to Dr. S. Sakakibara for supplying L-leucyl-L-tryptophan.

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