In vitro phosphorylation of purified transketolase by protein kinase C

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Title
In vitro phosphorylation of purified transketolase by protein kinase C
Author(s)
Yun Jo Soh; Kyu Shik Jeong
Bibliographic Citation
Molecules and Cells, vol. 6, no. 6, pp. 692-696
Publication Year
1996
Abstract
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 32P-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.
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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