抄録
In order to determine the properties of trehalase in the developing eggs of Bombyx mori, soluble-type trehalase was purified from the supernatant of egg homogenate by acid treatment, column chromatographies of Sephacryl S-300, DEAE-cellulofine and Con A-Sepharose, and preparative polyacrylamide gel electrophoresis. Two peaks of trehalase activity were detected by gel filtration column chromatography, and designated as P I (73kDa) and P II (140kDa). P I and P II were eluted as a single peak from ion exchange column chromatography at about 0.2M and 0.25M of NaCl, respectively. Subunit molecular masses of P I and P II were estimated as approximately 64kDa on SDS-PAGE and Western blot analysis. P I had a Km of 1.56mM for trehalose and an optimal pH around 6.5 with an activation energy of 11.03kCal/mol. P II had a Km of 0.44mM for trehalose and an optimal pH around 5.5 with an apparently lower activation energy of 5.92kCal/mol. These results suggest that two types of soluble trehalase are present in the embryonic larvae of the silkworm, Bombyx mori.
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