The complete amino acid sequence of the follitropin beta-subunit of the bullfrog, Rana catesbeiana.
The amino acid sequence of the bullfrog, Rana catesbeiana, follitropin beta-subunit has been determined by sequencing the intact protein (residues 1-39) and peptides originated by lysyl endopeptidase and pepsin. Twelve cysteine residues and two sugar chain binding sites at Asn-5 and Asn-22 are positional identities with bullfrog and mammalian beta-subunits. The bullfrog FSH beta-subunit is composed of 107 amino acid residues with a molecular mass of 11,782 Da, including the six cystine bridges and excepting the sugar chain. The bullfrog FSH beta-subunit has approximately 60% sequence identity with that of mammals and 40% with the fish gonadotropin beta-subunit. Conserved sequences among mammals (residue numbers 33-55 and 66-71) extensively differed from those of the bullfrog.
Hayashi
T
T
Institute of Endocrinology, Gunma University, Maebashi, Japan.
Hanaoka
Y
Y
Hayashi
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D010450:Endopeptidases; D005640:Follicle Stimulating Hormone / Q000032:analysis*; D005947:Glucose / Q000737:chemistry; D006062:Gonadotropins / Q000032:analysis; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010434:Pepsin A; D010455:Peptides / Q000032:analysis; D011892:Rana catesbeiana; D009626:Terminology as Topic
D000596:Amino Acids; D006062:Gonadotropins; D010455:Peptides; D005640:Follicle Stimulating Hormone; D010450:Endopeptidases; D010434:Pepsin A; D005947:Glucose