Abstract
An insoluble factor capable of binding Ca 2+ with high affinity has been obtained in 100-fold purification from water extracts of rat liver mitochondria. It contains a major protein species of MW ∼ 67,000 ± 10%, 27 percent phospholipid, free fatty acids, over 8 per cent hexosamines, and considerable chloroform-methanol insoluble phosphorus. It binds up to 70 nmoles of Ca 2+ per mg protein at high-affinity sites and about 900 nmoles of Ca 2+ at low affinity sites. Ca 2+ binding is inhibited by La 3+ and ruthenium red, but not by respiratory inhibitors or uncouplers. Dialysis in the presence of Ca 2+ inactivates Ca 2+ binding. The factor is compared with a soluble glycoprotein of ox liver mitochondria isolated by Sottocasa et, al. (4).
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