Hirotaka Kakita, Hiroshi Kamishima, Kuniyo Inouye
Purification and some properties of a d-fructose-1,6-bisphosphate aldolase from the red alga, Gracilaria chorda Holmes
D-Fructose-1,6-bisphosphate aldolase (0.042 mg) was purified from a red alga, Gracilaria chorda, by ammonium sulfate precipitation, followed by ion exchange and hydrophobic interaction chromatographies. The enzyme was purified 87-fold resulting in a final specific activity of 10.7 units/mg and a homogeneous appearance on electrophoresis. By SDS-PAGE analysis of the enzyme, two protein bands corresponding to molecular masses of 45 kDa and 39 kDa were observed. The enzymic activity disappeared in the presence of 0.5 mM EDTA, but was restored to 109% of the original untreated activity by the addition of 1 mM ZnSO4 subsequent to EDTA treatment. The enzyme was activated up to 5.5 times the original untreated activity by the addition of 500 mM KCl, and had a narrow optimum pH around 7.2. On the basis of these results, the G. chorda D-fructose-1,6-bisphosphate aldolase was characterized as a class II aldolase.
Botanica Marina, Walter de Gruyter
Print ISSN: 0006-8055
Volume: 49, 04/2006
Pages: 174 - 181
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