| Abstract: | A metal ion-activated acid ATPase was present in chicken liver lysosomes. We used Zn2+ as an activator. Lysosomal extract containing octylglucoside from chicken liver was centrifuged at 100,000 xg for 60 min. The supernatant was analyzed by gel filtration on a Sepharose 6B column. Two peaks of metal ion-activated acid ATPase activities were obtained according to the distribution patterns. Each of the two active fractions was incubated with phosphatidylinositol-specific phospholipase C at 37 degrees C for 60 min. The resulting solution was analyzed by gel filtration on a smaller size column of Sepharose 6B again. Molecular weight of the major peak was altered from approx. 1,600,000 to 130,000, whereas that of the minor one, 700,000, remained unchanged. |
