Insulin rapidly stimulates phosphorylation of a 46-kDa membrane protein on tyrosine residues as well as phosphorylation of several soluble proteins in intact fat cells.

Lignende værker

• Decreased tyrosine kinase activity of insulin receptor isolated from rat adipocytes rendered insulin-resistant by catecholamine treatment in vitro.
  af: Häring, H, et al.
  Udgivet: (1986)
• Insulin activates GTP binding to a 40 kDa protein in fat cells.
  af: Kellerer, M, et al.
  Udgivet: (1991)
• An Mr 180,000 protein is an endogenous substrate for the insulin-receptor-associated tyrosine kinase in human placenta.
  af: Machicao, F, et al.
  Udgivet: (1987)
• Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.
  af: Guan, J L, et al.
  Udgivet: (1991)
• Tyrosine phosphorylation of a yeast 40 kDa protein occurs in response to mating pheromone.
  af: Ballard, M J, et al.
  Udgivet: (1991)