Binding of filamin isoforms to myofibrils.

摘要: Two filamin isoforms were purified from bovine tissues and characterized. Muscle nonmuscle had different SDS gel mobilities, proteolytic digestion patterns, myofibrillar binding distributions myofibril affinities. The muscle specific an apparent molecular weight of 265 kDa bound primarily to the Z-lines myofibrils but also I-bands near Z-lines. 275 exclusively myofibrils. filamin–myofibril was studied quantitatively. Plotting fraction (mg filamin/mg myofibril) vs. equilibrium concentration free yielded a biphasic curve. first hyperbolic phase described second appeared be nonspecific due aggregation. significantly lower (P < 0.05) affinity than filamin. However, showed higher saturation value for phosphorylated corresponding native proteins both isoforms.