Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes from Turbo cornutus

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Physicochemical properties of the isozymes SP1 and SP2 of alginate lyase specific for poly-D-mannuronatewere investigated to elucidate their molecular sizes and shapes and conformational features. The molecular weight of each isozyme was about 25, 000 by ultracentrifugal analysis. This value was in good agreement with those from gel filtration experiments, and the sedimentation coefficients, s20, w, were 3.0S for SP1 and 3.1S for SP2. The partial specific volumes, diffusion coefficients, frictional ratios and Stokes radii were calculated by routine methods. These results suggested that the shape of the protein molecule of each isozymewasspherical. The circular dichroic spectra and optical rotatory dispersion showedthat the ordered structure of each isozyme molecule was most likely β-sheets. A more rigid conformation of SP2 than SP1 was observed by denaturation experiments and fluorescence properties.
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