Abstract
MORE than one component of human caeruloplasmin has been reported by several investigators1. Morell and Scheinberg1 have observed 4, possibly 5, components of caeruloplasmin by fractionating a pool composed of 9,109 individual sera. In such a large pool, infrequent unusual components would be easy to lose. Furthermore, the complex fractionation procedure provides opportunity for artefactual alteration of specific proteins. The resolving power of vertical starch-gel electrophoresis2 combined with direct chemical and enzymic analysis on the gel provides a simple and elegant means of examining the problem in individual sera. Using this technique we have found 5 electrophoretically distinct proteins having one or more characteristic properties of caeruloplasmin.
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