Characterization of Pituitary and Peptide Hormones by Electrophoresis in Starch Gel

Autor: Henry Friesen, E.B. Astwood, Richard J. Barrett
Rok vydání: 1962
Předmět:
Zdroj: Journal of Biological Chemistry. 237:432-439
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93939-6
Popis: SUMMARY A variety of pituitary and other protein hormone preparations exhibited characteristic patterns in starch gel electrophoresis, with the Ferguson and Wallace modification of Poulik’s discon- tinuous buffer system. Five human growth hormone prepara- tions prepared by different methods appeared similar. The four major bands in human growth hormone were inseparable from the four major bands in three different ovine prolactin preparations. Human prolactin shared two major bands in common with both human growth hormone and ovine prolactin. Human, simian, and porcine growth hormone shared three major bands in common, indistinguishable from one another, even with change in pH and prolonged electrophoresis. The simian prepa- ration had one and the porcine preparation four major compo- nents not detected in the human preparation. Purified bovine growth hormone had no bands in common with the other three preparations. Among the melanocyte-stimulating hormones (MSH) , syn- thetic (r-MSH (Hofmann) had the identical electrophoretic mobility as the major component in Schally’s preparation. The characteristic pattern of corticotropin A1 and AQ and ar-MSH and /I-MSH was established; a variety of corticotropin prepara- tions were examined, and the content of each of these peptides was assessed. Three purified parathyroid hormone preparations and two purified relaxin preparations were found not to be homogeneous
Databáze: OpenAIRE