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J. Biochem, 1982, Vol. 91, No. 4 1257-1265
© 1982 Japanese Biochemical Society

research-article

Chymotryptic Subfragments of Troponin T from Rabbit Skeletal Muscle. I. Determination of the Primary Structure1

Masaru TANOKURA2, Yuriko TAWADA and Iwao OHTSUKI

Department of Pharmacology, Faculty of Medicine, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812

Chymotryptic subfragments from rabbit skeletal troponin T were purified using column chromatography. Molecular weight values on SDS gel electrophoresis, tryptophan contents, N- and C-terminal residues, and amino acid compositions were examined for each subfragment. Based on these findings, the positions of the subfragments in the sequence of troponin T were determined as follows: N-terminal acetylserine-l-tyrosine-158 for troponin T1 (MW 18,700); serine-156—C-terminal lysine-259 for troponin T2{alpha}3 (MW 12,200); leucine-159—C-terminal lysine-259 for troponin T2 (or troponin T2{alpha}) (MW 11,900); leucine-159—phenylalanine-242 for troponin T2ßI (MW 10,200); leucine-159—tyrosine-227 for troponin T2ßII (MW 8,400); leucine-159-leucine-222 for troponin T2ßIII (MW 7,700); and serine-243—C-terminal lysine-259 for troponin T2{gamma} (MW 1,800).

The pathway of chymotryptic digestion of troponin T was also investigated and the results are discussed in relation to the higher structure of troponin T. The interaction of some chymotryptic subfragments with tropomyosin was also investigated by affinity chromatography.

1This work was supported in part by research grants from the Muscular Dystrophy Association, Inc., the Ministry of Education, Science and Culture of Japan, and National Center for Nervous, Mental and Muscular Disorders of the Ministry of Health and Welfare, Japan (No. 8001).

2Present address: Department of Physiology, Medical College of Oita, Oita, Oita 870-90.


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