Correlation between phosphorylation and kinase activity of a tyrosine protein kinase: p56lck

Biochem Biophys Res Commun. 1987 Nov 30;149(1):56-64. doi: 10.1016/0006-291x(87)91604-4.

Abstract

P56lck is the product of a cellular oncogene highly expressed in lymphoid cells. Tyrosine kinase activity was measured by using an exogenous substrate: polyamino acid glutamic acid-tyrosine (4:1) (PGT). Different levels of phosphorylation of p56lck were achieved by the utilisation of SH reagents and different lengths of incubation time. The phosphorylation of PGT was proportional to the level of phosphorylation of p56lck. Identical results were obtained with crude membrane preparations and with p56lck partially purified on immunecomplexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Cell Membrane / drug effects
  • Cell Membrane / enzymology
  • Ethylmaleimide / pharmacology
  • Immunosorbent Techniques
  • Intercellular Signaling Peptides and Proteins
  • Lymphoma / enzymology
  • Mercaptoethanol / pharmacology
  • Mice
  • Peptides / metabolism
  • Phosphates / metabolism
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins / metabolism*
  • Tumor Cells, Cultured

Substances

  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • Phosphates
  • Proto-Oncogene Proteins
  • L-glutamic acid-L-tyrosine copolymer
  • Mercaptoethanol
  • Adenosine Triphosphate
  • Protein-Tyrosine Kinases
  • Ethylmaleimide