scholarly journals Primary structure of rabbit skeletal muscle troponin-T. Purification of cyanogen bromide fragments and the amino acid sequence of fragment CB2.

1977 ◽  
Vol 252 (3) ◽  
pp. 971-977 ◽  
Author(s):  
J R Pearlstone ◽  
M R Carpenter ◽  
L B Smillie
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Cyanogen Bromide ◽  
Troponin T ◽  
Rabbit Skeletal Muscle

scholarly journals The amino acid sequence of troponin I from rabbit skeletal muscle

1975 ◽  
Vol 149 (2) ◽  
pp. 493-496 ◽  
Author(s):  
J M Wilkinson ◽  
R J A. Grand
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Troponin I ◽  
Rabbit Skeletal Muscle ◽  
British Library ◽  
Amino Acid Residues ◽  
N Terminus

The complete amino acid sequence of rabbit skeletal muscle troponin I was determined by the isolation of the cyanogen bromide fragments and the tryptic methionine-containing peptides. Troponin I contains 179 amino acid residues and has a molecular weight of 20864. Its N-terminus is acetylated. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50055 (23 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

scholarly journals The primary structure of troponin T and the interaction with tropomyosin

1975 ◽  
Vol 151 (1) ◽  
pp. 85-97 ◽  
Author(s):  
P Jackson ◽  
G W Amphlett ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Troponin T ◽  
Troponin C ◽  
The Other ◽  
Tryptic Digestion ◽  
Partial Digestion ◽  
Common Sequence

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.

Amino Acid Sequence of Acylphosphatase from Rabbit Skeletal Muscle

1985 ◽  
Vol 97 (4) ◽  
pp. 1155-1161 ◽  
Author(s):  
Takako KIZAKI ◽  
Toshihide TAKASAWA ◽  
Yusuke MIZUNO ◽  
Hiroyuki SHIOKAWA
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rabbit Skeletal Muscle
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