Identification of the native form of chicken gizzard myosin light chain kinase with the aid of monoclonal antibodies

1983 ◽  
Vol 115 (3) ◽  
pp. 855-863 ◽  
Author(s):  
Kazuo Adachi ◽  
Cheryl A. Carruthers ◽  
Michael P. Walsh
1984 ◽  
Vol 218 (3) ◽  
pp. 863-870 ◽  
Author(s):  
P K Ngai ◽  
C A Carruthers ◽  
M P Walsh

A simple and rapid procedure for the purification of the native form of chicken gizzard myosin light-chain kinase (Mr 136000) is described which eliminates problems of proteolysis previously encountered. During this procedure, a calmodulin-binding protein of Mr 141000, which previously co-purified with the myosin light-chain kinase, is removed and shown to be a distinct protein on the basis of lack of kinase activity, different chymotryptic peptide maps, lack of cross-reactivity with a monoclonal antibody to turkey gizzard myosin light-chain kinase, and lack of phosphorylation by the purified catalytic subunit of cyclic AMP-dependent protein kinase. This Mr-141000 calmodulin-binding protein is identified as caldesmon on the basis of Ca2+-dependent interaction with calmodulin, subunit Mr, Ca2+-independent interaction with skeletal-muscle F-actin, Ca2+-dependent competition between calmodulin and F-actin for caldesmon, and tissue content.


Biochemistry ◽  
1978 ◽  
Vol 17 (2) ◽  
pp. 253-258 ◽  
Author(s):  
Renata Dabrowska ◽  
James M. F. Sherry ◽  
Debra K. Aromatorio ◽  
David J. Hartshorne

1990 ◽  
Vol 87 (6) ◽  
pp. 2284-2288 ◽  
Author(s):  
N. J. Olson ◽  
R. B. Pearson ◽  
D. S. Needleman ◽  
M. Y. Hurwitz ◽  
B. E. Kemp ◽  
...  

Biochemistry ◽  
1986 ◽  
Vol 25 (26) ◽  
pp. 8372-8381 ◽  
Author(s):  
Vince Guerriero ◽  
Mario A. Russo ◽  
Norma J. Olson ◽  
John A. Putkey ◽  
Anthony R. Means

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