Domain organization of alpha-actinin from the rabbit skeletal muscle
Kuridze, K.S.; Ven'iaminov, S.I.; Simonidze, M.S.; Nadirashvili, N.S.; Zaalishvili, M.M.
Biokhimiia 53(6): 899-904
1988
ISSN/ISBN: 0320-9725 PMID: 3179351 Document Number: 316362
Limited trypsinolysis of native alpha-actinin by trypsin was carried out. This procedure resulted in the formation of two large fragments with Mr of 30 and 70 kD which cover almost the whole subunit of alpha-actinin. Using the sedimentation equilibrium method, it was demonstrated that the bisubunit structure of alpha-actinin is provided for by C-terminal fragments of the subunits. Data from circular dichroism analysis suggest that the fragments formed are independent structural units, i.e., domains.