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.
Kobayashi
T
T
Department of Biology, School of Education, Waseda University, Tokyo, Japan.
Kikuyama
S
S
Yasuda
A
A
Kawauchi
H
H
Yamaguchi
K
K
Yokoo
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002356:Cartilage / Q000187:drug effects; D013006:Growth Hormone / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D008969:Molecular Sequence Data; D010903:Pituitary Gland, Anterior / Q000032:analysis*; D011892:Rana catesbeiana; D013249:Sternum / Q000187:drug effects; D014981:Xenopus
D000596:Amino Acids; D013006:Growth Hormone