On the Subunit Structure of the Cold Labile Adenosine Triphosphatase of Mitochondria

摘要: Abstract Mitochondrial ATPase has been studied by equilibrium ultracentrifugation. Under virtually all conditions examined, the oligomeric structure (mol. wt. 2.8 x 105) is in with smaller polypeptide chains. In dilute buffer, however, proportion of dissociated subunits become appreciaable only cold (5°). At this temperature, molecular weight can be measured directly, and a value 4.6 104 obtained. Additional experiments solutions guanidine hydrochloride (6 to 9 m) indicate that no further dissociation beyond unit occurs. The results are evaluated terms probably hexameric for ATPase.