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

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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.