Abstract
Abstract The increased alkaline phosphatase (EC 3.1.3.1) activity of reconstituted lyophilized control sera has recently been the focus of considerable interest because of its possible implications for quality-control procedures. We confirm that these reconstituted materials show a temperature-dependent increase in alkaline phosphatase activity, but could show no alteration in activity of fresh sera. The rate of increase in activity was unaffected by dialysis of the reconstituted material, and occurred more rapidly in dilute solutions. Studies with acrylamide gel electrophoresis and Sephadex G-200 gel filtration showed that, immediately after reconstitution, a high-molecular-weight alkaline phosphatase component predominated; during subsequent spontaneous activation this component decreased, and there was a concomitant increase in a low-molecular-weight alkaline phosphatase component. The results obtained when the reconstituted material was extracted with butanol suggest that the observed changes in alkaline phosphatase activity may be attributed to the breakdown of a complex between alkaline phosphatase and lipoprotein.
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