作者: G.A. Boffa , B. Martin , J.J. Winchenne , R. Ozon
DOI: 10.1016/S0300-9084(72)80018-X
关键词: Steroid 、 Biochemistry 、 Hormone 、 Testosterone 、 Transferrin 、 Globulin 、 Sex steroid 、 Corticosterone 、 Biology 、 Transcortin
摘要: Summary 1. Steroid-protein interactions in Amphibians and Cyclostoma sera are studied by analytical ion exchange chromatography electrophoresis associated to autoradiography. As higher vertebrates these species possess proteins with high steroid affinity. 2. Our results confirmed that three binding occured human sera. SBP is a β globulin which possesses affinity for testosterone estradiol-17 β. CBG or α 1 -α 2 smaller than compounds. 3. Two present Pleurodele (Amphibian). One sex (SBP). The second one low concentration binds corticosterone. This protein can be compared the mammalian transcortin. electronegative charge of this weaker according its DEAE cellulose behaviour. transferrin distinguished electrophoretic chromatographic patterns. 4. also found Lamprey (Cyclostoma) : an globulin. Progesterone show marked two components but progesterone preferentially bound In specificity less restrictive even Amphibian SBP. clearly separated from transferrin. — corticosterone complexes more affected temperature those formed progesterone. able fo bind hormones, seems wider Albumine-α third system it revealed autoradiography [ 14 C].