In the late 60’s investigators in two laboratories reported the discovery of a specific pregnancy protein in the uterine fluid of the rabbit. Krishnan and Daniel (1967) isolated from the uterus of the rabbit at early pregnancy a protein fraction that seemed to induce blastulation of the rabbit morula and to stimulate blastocyst development; it was, therefore, named blastokinin. Early purification resulted in what was considered a homogeneous glycoprotein of MW 27,000 (Krishnan and Daniel 1968). Independently of this work, Beier (1968 a) described a protein from rabbit uterine fluid, called uteroglobin, that did not seem to contain carbohydrate and was believed to have a MW of about 30,000. Later studies under more rigorously controlled conditions using gel filtration and equilibrium sedimentation resulted in a lower MW of about 15,000 (Murray et al. 1972). The absence of carbohydrate was confirmed more recently in highly purified uteroglobin (Nieto et al. 1977; Torkkeli et al. 1978). The investigators principally involved in the beginning of uteroglobin research have reviewed their work in detail (Beier et al. 1971; Beier 1976; Daniel 1971; 1976).
KeywordsRelative Binding Affinity Uterine Lumen Uterine Fluid Male Genital Tract Chlormadinone Acetate
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