Biomedical Science Letters (대한의생명과학회지)
- Volume 2 Issue 1
- /
- Pages.21-30
- /
- 1996
- /
- 1738-3226(pISSN)
- /
- 2288-7415(eISSN)
Purification and Characterization of Mitogen -Activated Protein (MAP) Kinase from Mammalian Tissue Cells
동물 조직세포로부터 Mitogen-activated Protein (MAP) Kinase의 분리 및 성격규명
Abstract
MAP kinases are a family of serine/threonine specific protein kinases becoming activated in response to different proliferative stimuli by phosphorylation at both threonine and tyrosine residue. Present study shows that MAP kinase was purified from P388 murine leukema cells by SP sephadex C-50, phenyl superose and Mono Q column chromatography and identified with anti-ERKl antibody by western blotting. Immnublotting analysis to the crude extract of P388 cell lysate shows 44 kD and other minor bands but partial purified fraction eluted from phenyl supherose column have 44kD and 66 kD isoform. Subcloned GST-fusion protein from N-terminal of
Mitogen-activated protein (MAP) kinase는 여러 세포증식 촉진인자들에 의하여 자신이 인산화됨으로써 활성화되어 다른 protein kinase를 인산화시키는 역할을 하는 세포내 신호전달의 중요한 효소이다. 본 연구에서는 P388 murine leukemia 세포 파쇄액에서 SP sephadex C-50, phenyl superose, Mono Q column을 통하여 MAP kinase를 분리한 결과, 44 kD와 66kD의 isoform을 확인할 수 있었다. 면역 T 세포의