Determination of the Ca2+ and Mg2+ affinity constants of troponin C from eel skeletal muscle and positioning of the single tryptophan in the primary structure

1993 ◽  
Vol 14 (6) ◽  
pp. 585-593 ◽  
Author(s):  
Jean-Marie Fran�ois ◽  
Charles Gerday ◽  
Franklyn G. Prendergast ◽  
James D. Potter
1975 ◽  
Vol 151 (1) ◽  
pp. 85-97 ◽  
Author(s):  
P Jackson ◽  
G W Amphlett ◽  
S V Perry

1. Eight peptides were separated from the CNBr digest of troponin T from rabbit white skeletal muscle and characterized. 2. By study of the amino acid sequence of the methionine-containing peptides isolated after chymotryptic and tryptic digestion and of the N- and C-terminals of the CNBr peptides, six of the latter were shown to be arranged in the sequence CNB1-CNB2-CNB5-CNB6-CNB8-CNB7. The other two peptides, CNB1′ and CNB3, have been shown to be partial digestion products. 3. The CNBr peptides CNB1′ and CNB2 contained a common sequence and were the only peptides in CNBr digests of troponin T that formed a complex with tropomyosin as judged by viscometric and electrophoretic studies. 4. It is concluded that tropomyosin interacts with the N-terminal half of the troponin T molecule approximately in the region lying between residues 70 and 160. 5. Electrophoretic evidence indicates that tropomyosin and troponin C interact with troponin T. 6. None of the major CNBr peptides of troponin T isolated formed a complex with troponin C on electrophoresis at pH 8.6.


1982 ◽  
Vol 257 (16) ◽  
pp. 9593-9597 ◽  
Author(s):  
M D Pierschbacher ◽  
E Ruoslahti ◽  
J Sundelin ◽  
P Lind ◽  
P A Peterson

Nature ◽  
1989 ◽  
Vol 339 (6224) ◽  
pp. 439-445 ◽  
Author(s):  
Hiroshi Takeshima ◽  
Seiichiro Nishimura ◽  
Takeshi Matsumoto ◽  
Hiroyuki Ishida ◽  
Kenji Kangawa ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document