Amphibian lutropin from the bullfrog Rana catesbeiana. Complete amino acid sequence of the beta subunit.
The amino acid sequence of lutropin (LH) beta subunit of an amphibian, the bullfrog Rana catesbeiana, has been determined. The primary structure was determined by sequencing the intact protein (residues 1-44) and peptides originated by cyanogen bromide cleavage and lysyl endopeptidase digestion. 12 cysteine residues are conserved in the bullfrog and mammalian LH beta subunit. One sugar-chain-binding site at Asn-8 is also conserved in the bullfrog and in all mammals except humans. This glycoprotein is composed of 112 amino acid residues with a molecular mass of 12675 Da, considering the six cystine bridges and excepting the sugar chain. The bullfrog beta subunit has approximately 50% sequence identity with that of mammals and with the fish gonadotropin beta subunit, and about 40% with bullfrog follicle-stimulating hormone beta subunit.
Hayashi
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Institute of Endocrinology, Gunma University, Maebashi, Japan.
Hayashi
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Hanaoka
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Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D006801:Humans; D007986:Luteinizing Hormone / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011892:Rana catesbeiana; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000378:metabolism
D000596:Amino Acids; D010446:Peptide Fragments; D007986:Luteinizing Hormone; D012697:Serine Endopeptidases; C036813:lysyl endopeptidase; D003488:Cyanogen Bromide