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KMID : 0578319960060060692
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Molecules and Cells
1996 Volume.6 No. 6 p.692 ~ p.696
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In Vitro Phosphorylation of Purified Transketolase by Protein Kinase C
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Soh Yunjo
Jeong Kyu-Shik
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Abstract
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Catalytically active transketolase was purified from rat liver cytosolic fraction by more than 120-fold to near homogeneity by successive column chromatography using DEAE-Sephacel, hydroxylapatite and Mono P matrices. The purified transketolase was rapidly phosphorylated by protein kinase C (PKC) while it was minimally phosphorylated by cAMP-dependent protein kinase and casein kinase Ⅱ. Phosphoamino acid analysis of the ^(32)p-labeled enzyme revealed that only threonine residue was phosphorylated by PKC. The phosphorylated enzyme became less active (about 40%) than the non-phosphorylated counterpart. Our data suggest that transketolase can be phosphorylated by PKC, which could represent a new type of regulatory mechanism for transketolase.
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KEYWORD
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