Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle.
Journal Article (Journal Article)
Mitogen-activated protein kinase (MAP kinase) activator was purified 2000-fold from skeletal muscle, and proteins which co-purified with the activator were analysed after SDS/PAGE by renaturation and partial sequencing. Activity for tyrosine and threonine phosphorylation of MAP kinase was present in two bands of approx. 48 and 46 kDa, which have sequence similarity to small GTP-binding protein p25 GDP dissociation inhibitor and protein kinases (PBS2, SPK1+, STE7, BYR1) respectively.
- Wu, J; Michel, H; Rossomando, A; Haystead, T; Shabanowitz, J; Hunt, DF; Sturgill, TW
- August 1, 1992
Volume / Issue
- 285 ( Pt 3) / Pt 3
Start / End Page
- 701 - 705
Pubmed Central ID
International Standard Serial Number (ISSN)
Digital Object Identifier (DOI)