Arylsulfatase from Sphingomonas sp. nov. was purified through ionic exchange chromatography and gel filtration. The molecular weight of the enzyme was estimated to be 64 kDa by SDS-PAGE. The enzyme showed an optimum reaction condition at pH 7.0 and 45•Ž. With the reaction of agar with arylsulfatase in the ratio of 1:10-6 (w/w) for 2 hr at 50•Ž, gel strength of agar was increased to 2.3 fold and 97% (p<0.01) of sulfate in agar was removed. The result suggests that arylsulfatase could be applicable to the production of value-added products such as electrophoretic grade agarose.
In this study, we focused on myomoduline A (MMA) released from the central nervous system of Aplysia kurodai. The primary structure of MMA is Pro-Met-Ser-Met-Leu-Arg-Leu-NH2. This peptide is the same as that of the myomodulin family peptide found in other mollusks. The purified MMA showed a modulating activity of phasic contraction on the anterior byssus retractor muscle (ABRM) of Mytilus edulis. In order to study the relationship between the structure and biological activity of
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