作者: H. Kosako , Y. Gotoh , S. Matsuda , M. Ishikawa , E. Nishida
DOI: 10.1002/J.1460-2075.1992.TB05359.X
关键词:
摘要: Xenopus MAP kinase activator, a 45 kDa protein, has been shown to function as direct upstream factor sufficient for full activation and both tyrosine serine/threonine phosphorylation of inactive kinase. We have now by using an anti-MAP activator antiserum that is ubiquitous in tissues regulated post-translationally. Activation correlated precisely with its threonine during the oocyte maturation process. It key question whether or not. purified from mature oocytes capable undergoing autophosphorylation on serine, residues. Dephosphorylation protein phosphatase 2A treatment inactivates activity well activity. Thus, specificity tyrosine. Partial sequencing indicates it contains sequence homologous subdomains VI VII two yeast kinases, STE7 byrl.