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XB-ART-26885
Gen Comp Endocrinol 1989 Mar 01;733:417-24. doi: 10.1016/0016-6480(89)90199-8.
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Purification and characterization of bullfrog growth hormone.

Kobayashi T , Kikuyama S , Yasuda A , Kawauchi H , Yamaguchi K , Yokoo Y .


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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.

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Species referenced: Xenopus
Genes referenced: prl.1