RESOLUTION D'UNE PREPARATION GONADOTROPE SERIQUE DE JUMENT GRAVIDE EN PLUSIEURS CONSTITUANTS ET PURIFICATION PAR ELECTROPHORESE DE ZONE SUR AMIDON

Abstract

The components of the homogeneous gonadotrophin could be reconstituted into the original protein with the same electrophoretic mobility. In the original preparation the hormone is in the form of a dissociable protein complex. The heterogeneous hormone was isolated through zone-electrophoresis on starch and was shown to be electrophoretically homogeneous in the Tiselius apparatus, in a wide range of pH. The isoelectric point of this preparation (pH = 1.8) is distinctly different from that of the initial preparation, which is equivalent to 2.65. In the heterogeneous preparation, one boundary alone is responsible for the double follicle-stimulating hormone (FSH) and luteinizing hormone (LH) activity.