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KMID : 0380219940270060538
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 6 p.538 ~ p.543
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Purification and General Properties of Pea Cytoplasmic Fructose-1, 6-bisphosphates
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Abstract
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Abstract:
@EN Cytoplasmic fructose-l,6-bisphosphatase(FBPase) from pea leaves was purified and characterized. The purified enzyme appeared to be homogeneous with a monomeric molecular weight of 37,000 as determined by SDS polyacrylamide gel
electrophoresis.
The
purified enzyme was active at neutral pH(pH 6.0 to pH 7.0) and insensitive to dithiothreitol, as are other gluconeogenic FBPases from mammals and yeast. It was relatively stable stable against heat. The activation energy (Ea) and the Arrhenius
frequency
factor of the enzyme catalyzed reaction 8.75 kcal/mol and 1.8×10E4/s, respectively.
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KEYWORD
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