Isolation and Properties of CBG from Mammalian Sera

Abstract

It is apparent from the preceding chapters that the very low blood concentration and the limited stability of CBG make it difficult to isolate. The first investigators to succeed were Seal and Doe (1961) who reported at the 1961 Federation Meeting the preparation of highly purified CBG from serum of estrogen-treated males. In this pioneering work, an overall recovery of 80% after approximately 1000-fold purification was obtained; physicochemical characterization revealed the properties of a glycoprotein with the characteristics of an α₁-globulin. One of the more important steps for the separation from other serum proteins was the chromatography on hydroxylapatite which did not adsorb CBG but retained most other proteins. A detailed account of the results was given subsequently (Seal and Doe, 1962 a, 1962 b). Partial purification of human CBG has been briefly reported by Ensinck and Volwiler (1962).