Interaction of the calcium and calmodulin regulated eEF-2 kinase with heat shock protein 90.
Immunoadsorbents containing the 8D3 anti-heat shock protein 90 monoclonal antibodies were prepared. Partly purified preparations of the Ca2+ and calmodulin dependent eukaryotic elongation factor eEF-2 specific kinase and crude rabbit reticulocyte lysates were mixed with the immunoadsorbent. After removal of unbound proteins the adsorbed material was released by increasing the salt concentration in the buffer. Analysis of the bound material showed that the eEF-2 kinase was bound to the immunoadsorbent together with hsp 90. The adsorption of the kinase was found to depend on the presence of hsp 90.
Palmquist
K
K
Department of Zoological Cell Biology, Arrhenius Laboratories E5, Stockholm University, Sweden.
Riis
B
B
Nilsson
A
A
Nygård
O
O
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis; D002118:Calcium / Q000378:metabolism*; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D054736:Elongation Factor 2 Kinase; D006041:Goats; D006360:Heat-Shock Proteins / Q000378:metabolism*; D011817:Rabbits
D000911:Antibodies, Monoclonal; D002147:Calmodulin; D006360:Heat-Shock Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D054736:Elongation Factor 2 Kinase; D002118:Calcium