Cyanogen bromide fragments of Akazara scallop Mr 52,000 troponin-I.
Akazara scallop troponin-I of Mr 52,000 (52K) was cleaved into two fragments of 17K and 35K with cyanogen bromide. The 17K fragment, along with tropomyosin, inhibited weakly the rabbit actomyosin Mg-ATPase activity, however, the 35K fragment did not affect it at all. In the presence of Akazara scallop TnT (40K component), the 17K fragment, in turn, strongly inhibited the activity, while the 35K fragment did not. The amino acid composition and partial amino acid sequence suggested that the 17K and 35K fragments were derived from C- and N-terminal regions of the TnI, respectively, and that structural similarity to TnIs from other animals is present in the 17K region.
Ojima
T
T
Department of Chemistry, Faculty of Fisheries, Hokkaido University.
Tanaka
H
H
Nishita
K
K
D000596:Amino Acids / Q000032:analysis; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D003488:Cyanogen Bromide; D008970:Molecular Weight; D012758:Shellfish / Q000032:analysis*; D014336:Troponin / Q000737:chemistry* / Q000378:metabolism; D019210:Troponin I
D000596:Amino Acids; D014336:Troponin; D019210:Troponin I; D017301:Ca(2+) Mg(2+)-ATPase; D003488:Cyanogen Bromide