[Domain organization of alpha-actinin from the rabbit skeletal muscle].
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.
Kuridze
K Sh
KSh
Ven'iaminov
S Iu
SIu
Simonidze
M Sh
MSh
Nadirashvili
N Sh
NSh
Zaalishvili
M M
MM
D000185:Actinin / Q000032:analysis* / Q000648:ultrastructure; D000818:Animals; D002942:Circular Dichroism; D006868:Hydrolysis; D008854:Microscopy, Electron; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D011487:Protein Conformation; D011817:Rabbits
D000185:Actinin
Domennaia organizatsiia alpha-aktinina skeletnoĭ myshtsy krolika.