The amino acid sequences of the prepeptides contained in the alpha and beta subunits of human choriogonadotropin

J Biol Chem. 1981 Feb 25;256(4):1816-23.

Abstract

The amino acid sequences of the NH2-terminal extension prepeptides of the alpha and of the beta subunits of human choriogonadotropin have been determined by translation of first trimester placental mRNA in the presence of individually labeled amino acids. The structure of the prepeptide of the alpha subunit is: -24 -23 -22 -21 -20 -19 -18 -17 -16 -15 Met- Asp- Tyr- Tyr- Arg- Lys- Tyr- Ala- Ala- Ile -14 -13 -12 -11 -10 -9 -8 -7 -6 -5 Phe- Leu- Val- Thr- Leu- Ser- Val- Phe- Leu- His -4 -3 -2 -1 Val- Leu- His- Ser The structure of the prepeptide of the beta subunit is: -20 -19 -18 -17 -16 -15 -14 -13 -12 -11 Met- Glu- Met- Phe- Gln- Gly- Leu- Leu- Leu- Leu -10 -9 -8 -7 -6 -5 -4 -3 -2 -1 Leu- Leu- Leu- Ser- Met- Gly- Gly- Thr- XXX- Ala In the presence of membranes, the beta prepeptide is cleaved to a protein containing the authentic NH2-terminal sequence of the secreted form of the beta subunit. Cleavage of pre-alpha subunit also yields a product containing the NH2-terminal region of the secreted form.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chorionic Gonadotropin* / biosynthesis
  • Female
  • Humans
  • Macromolecular Substances
  • Peptide Fragments / analysis
  • Placenta / metabolism
  • Pregnancy
  • Protein Biosynthesis
  • Protein Precursors* / biosynthesis
  • RNA, Messenger / metabolism

Substances

  • Chorionic Gonadotropin
  • Macromolecular Substances
  • Peptide Fragments
  • Protein Precursors
  • RNA, Messenger