Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle.
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
J
Department of Medicine, University of Virginia, Charlottesville 22908.
Michel
H
H
Rossomando
A
A
Haystead
T
T
Shabanowitz
J
J
Hunt
D F
DF
Sturgill
T W
TW
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D005260:Female; D013058:Mass Spectrometry; D020929:Mitogen-Activated Protein Kinase Kinases; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000737:chemistry*; D010766:Phosphorylation; D010769:Phosphothreonine / Q000378:metabolism; D019000:Phosphotyrosine; D011489:Protein Denaturation; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D010769:Phosphothreonine; D019000:Phosphotyrosine; D014443:Tyrosine; D011494:Protein Kinases; D020929:Mitogen-Activated Protein Kinase Kinases