상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

In vitro phosphorylation of purified transketolase by protein kinase C

Authors 

Yun Jo SohKyu Shik Jeong

Publisher 

Springer Verlag (Germany)

Issue Date 

1996

Citation 

Molecules and Cells, vol. 6, no. 6, pp. 692-696

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

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)