|
KMID : 0578319940040020177
|
|
Molecules and Cells
1994 Volume.4 No. 2 p.177 ~ p.181
|
|
|
Characterization of protein tyrosine Konase of v-yes Oncogene Expressed in Escherichia coli
|
|
Ahn, Sohyun
Lee, Eun-Jyeong/Hwang, Sang-Youn/Yang, Chul-Hak
|
|
|
Abstract
|
|
|
|
ti yes oncogene, a genomic segment of avian sarcoma virus (ASV) Y73, which encodes Src homology 3 (SH3), Src homology 2 (SH2), and protein tyrosine kinase (PTK) domains was amplified by PICK inserted into pFLAG-1 vector, and expressed as a soluble fusion protein to FLAG marker peptide in E coli Y-1. The 55 kDa protein was partially purified after ammonium sulfate precipitation and MonoQ FPLC column chromatography. Several properties of this p55y- were examined. The enzyme, p551e phosphorylated tyrosine residues on poly(Glu, Tyr)4,1 (PGT) and casein and K. and V.,.x values were determined. The enzyme showed an essential requirement for Me´ or Mn" with optifhal concentrations of 30 mM and 3 mM, respectively and a preference of Mgt+. The optimum pH was 7.4. The enzyme contained phosphotyrosine residues and could be further autophosphorylated in vitro in presence of ATP and Mgt+. This additional autophosphorylation resulted in increase in the kinase activity toward PGT and casein.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|