Amphibian lutropin and follitropin from the bullfrog Rana catesbeiana. Complete amino acid sequence of the alpha subunit.
The amino acid sequence of the alpha-subunit of the gonadotropins, lutropin and follitropin from bullfrog, Rana catesbeiana, has been determined. The alpha-subunit was identified in both hormones by the amino acid composition and ovulation activity of lutropin in the Xenopus ovary, by means of reconstituted hormones in various combinations. The amino acid sequences of two identical alpha-subunits from lutropin and follitropin were determined or deduced by different strategies. The alpha-subunit of those gonadotropins have 97 amino acid residues, the longest among the known alpha-subunits of gonadotropins, and one arginine insertion at position 29. Ten cysteine residues and two sugar-chain binding sites at Asn57 and Asn83 are completely conserved among the species. The molecular mass of this subunit is 11,026 Da not including the sugar chains. The bullfrog alpha-subunit has approximately 70% sequence identity with mammalian alpha-subunits.
Hayashi
H
H
Institute of Endocrinology, Gunma University, Maebashi, Japan.
Hayashi
T
T
Hanaoka
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D005260:Female; D005640:Follicle Stimulating Hormone / Q000235:genetics*; D007986:Luteinizing Hormone / Q000235:genetics*; D008969:Molecular Sequence Data; D010053:Ovary / Q000502:physiology; D010060:Ovulation; D011892:Rana catesbeiana; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin / Q000737:chemistry; D014981:Xenopus
D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone; D014357:Trypsin; D003488:Cyanogen Bromide