[Specific splitting of alpha-tropomyosin at cysteine-190 and a physico-chemical study of the fragments].

alpha-tropomyosin from rabbit spine muscle specifically cleaves at cystein-190. A study has been made of the physico-chemical parameters of the fragments resulting from the cleavage. The distortion of their structure by the cleavage is not great. The N- and C-end fragment are able to form a complex with an association constant of 5.10(4) M(-1). It is shown electrophoretically that troponin binds with the fragments only in the case when both fragments are present in the solution.