An Analysis of the Interaction of Sodium Dodecyl Sulfate with Lysozyme |
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Authors: | Taiji Imoto Shin-ichiro Sumi Masaharu Tsuru Kazuyoshi Yagishita |
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Affiliation: | 1. Faculty of Pharmaceutical Sciences, Kyushu University, Maidashi, Fukuoka 812, Japan;2. Laboratory of Biochemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753, Japan |
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Abstract: | The interaction of SDS with lysozyme was analyzed with enzyme activity and with NMR, fluorescence, and UV difference spectroscopies using various alkyl sulfates and variously modified lysozymes. SDS formed a stable complex with lysozyme without causing a gross conformational change in the enzyme molecule. Some SDS molecules bound to the active site cleft of lysozyme and therefore strongly inhibited the activity of lysozyme. Hydrophobic regions and positive charges for protein side, and a hydrophobic tail (possibly more than 8 carbons in alkyl chain) and a negative charge for detergent side were required for the formation of the complex. |
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Keywords: | radioactive soil radioactive Cs removal photosynthetic bacteria anaerobic digestion lactic acid fermentation |
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