Studies on the Growth Hormone-Like Factor Produced by Plerocercoids of Spirometra erinacei.

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In order to examine the physiological property and partial amino acid sequence of the Growth Hormone (GH) -like factor produced by plerocercoids of Spirometra erinacei, we tried to purify this factor detected bt radio-receptor assay for GH using the GH receptor-coupled affinity chromatography. The GH-like factor were purified.1) One of GH-like factor was purified by two steps consisted of the affinity chromatography and gel filtration.2) The specific activity in this GH-like factor was enhanced to 195 times compared with the specific activity in the crude worm extract.3) This factor exhibited the high affinity for the GH receptor and its molecular weight was estimated to be approximately 16 KD by SDS-polyacryl amide gel electrophoresis.4) This factor stimulated the prolifelation of the mouse hepatocyte in vitro, and then suppressed the serum level of glucose when this factor was injected into the femoral vein of a golden hamster compared with the control.5) This 16 KD protein obviously cross-reacted with anti-human GH monoclonal antibody on the immunoblot method.6) The 27 KD protein, which had low affinity for the GH receptor, was also purified from the worm extract and cross-reacted with anti-human GH-monoclonal antibody. Moreover, this stimulated the proliferation of the mouse hepatocyte in vitro.7) There was the homology of 67% between amino acid sequences of cathepsin L and the fragment of the 27 KD protein cleavaged by lysil endo peptidase.