Reevaluation of the amino acid sequence of porcine follitropin.
We have reevaluated the sequence of porcine follicle-stimulating hormone (pFSH) with more recent protein-sequencing methodology. This has led to revision of the earlier proposed sequence. As with almost all reported gonadotropin alpha-subunits, NH2-terminal heterogeneity was found in the porcine FSH alpha-subunit (FSH alpha), starting with residue Phe (1), Asp (3), Gly (4), or Thr (7). In the beta-subunit, there were found to be at least two molecular species, starting with residue Asn (1) (minor 20%) or Cys (3) (major 80%) as NH2-terminal and ending at residue Glu (108) as COOH-terminal. The net effect of the present revisions is to increase the homology of pFSH beta with other reported follitropin sequences. Apparent differences in the half-cystine placements in a previous proposal for pFSH beta compared with other species of FSH are no longer tenable. The half-cystine placements thus remain a constant structural feature throughout the gonadotropin hormones (choriogonadotropin, follitropin, and lutropin).
Sugino
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Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston 77030.
Takio
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K
Ward
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D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005640:Follicle Stimulating Hormone; D007202:Indicators and Reagents; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases; D013552:Swine
D007202:Indicators and Reagents; D046911:Macromolecular Substances; D005640:Follicle Stimulating Hormone; D010447:Peptide Hydrolases