[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.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis; D010446:Peptide Fragments; D011817:Rabbits; D014335:Tropomyosin; D014336:Troponin
D010446:Peptide Fragments; D014335:Tropomyosin; D014336:Troponin
Spetsificheskoe rasshcheplenie alpha-tropomiozina po tsisteinu-190 i fiziko-khimicheskoe izuchenie fragmentov.