Purification and characterization of bullfrog growth hormone.

A highly purified growth hormone (GH) was isolated from an unadsorbed fraction obtained by subjecting acid acetone extract of bullfrog pituitary glands to DEAE-cellulose column chromatography, a side fraction obtained during the purification of prolactin, by cation-exchange chromatography on CM-Toyopearl and high-performance liquid chromatography on ODS with a yield of 5.6 mg/g protein of the starting material. Intraperitoneal injections of GH to hypophysectomized Xenopus resulted in a considerable elevation of chondroitin sulfate synthesis in the xiphisternal cartilage as measured in vitro. The bullfrog GH had a molecular weight of 22,000 Da as determined by sodium dodecyl sulfate-gel electrophoresis. The isoelectric point of bullfrog GH was estimated to be 7.8 by gel electrofocusing. The partial amino acid sequences of bullfrog GH at both terminal regions were determined.