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J. Biol. Chem., Vol. 262, Issue 18, 8603-8609, Jun, 1987
H Sugino, GR Bousfield, WT Moore Jr and DN Ward
The complete amino acid sequence of the beta-subunit of equine chorionic
gonadotropin (eCG beta) has been established by both automated Edman and
manual 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradations. Specific
fragments were produced by cleavage with Staphylococcus aureus V8 protease,
trypsin, or dilute HCl. For the sequence analyses of the heavily
glycosylated COOH-terminal portion, a chemical deglycosylation procedure
with trifluoromethanesulfonic acid was employed. The peptide chain of eCG
beta consists of 149 amino acid residues. Five or more oligosaccharide
chains are attached to the protein, 1 unit linked by an N-glycosidic bond
to asparagine at residue 13 and four or more units linked by O-glycosidic
bonds to serine or threonine at residues in the COOH-terminal portion. The
carbohydrate- bearing hydroxy amino acids have not yet been rigorously
established. As compared to the beta-subunits of the pituitary gonadotropin
hormones, lutropin, follitropin, and thyrotropin, eCG beta possesses a
glycosylated COOH-terminal extension of about 30 amino acid residues, as
does the human chorionic gonadotropin beta-subunit (hCG beta). When the
comparison is restricted inside the disulfide bond-containing core
(residues 1-110), the beta-subunit of eCG is highly homologous to hCG beta
(66%). On the other hand, although the overall structural features closely
resemble each other, much less homology exists in the COOH- terminal
extensions of eCG beta and hCG beta.
Structural studies on equine glycoprotein hormones. Amino acid sequence of equine chorionic gonadotropin beta-subunit
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