Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle

Biochem J. 1992 Aug 1;285 ( Pt 3)(Pt 3):701-5. doi: 10.1042/bj2850701.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, Gel
  • Female
  • Mass Spectrometry
  • Mitogen-Activated Protein Kinase Kinases
  • Molecular Sequence Data
  • Molecular Weight
  • Muscles / chemistry*
  • Phosphorylation
  • Phosphothreonine / metabolism
  • Phosphotyrosine
  • Protein Denaturation
  • Protein Kinases / chemistry*
  • Protein Kinases / metabolism
  • Rabbits
  • Sequence Homology, Nucleic Acid
  • Tyrosine / analogs & derivatives
  • Tyrosine / metabolism

Substances

  • Phosphothreonine
  • Phosphotyrosine
  • Tyrosine
  • Protein Kinases
  • Mitogen-Activated Protein Kinase Kinases

Associated data

  • GENBANK/D10993
  • GENBANK/D10994
  • GENBANK/D13341
  • GENBANK/M86481
  • GENBANK/S46845
  • GENBANK/S46846
  • GENBANK/S46849
  • GENBANK/X65732
  • GENBANK/X65733
  • GENBANK/X65734