Human pituitary lutropin. Isolation, properties, and the complete amino acid sequence of the beta-subunit

Biochim Biophys Acta. 1975 Nov 18;412(1):70-81.

Abstract

The separation of alpha and beta subunits from human pituitary lutropin is described, and the complete amino acid sequence of the beta subunit is proposed. It consists of 115 amino acids with serine and glycine at the amino and carboxyl termini, respectively. The single carbohydrate moiety is linked to asparagine in position 30 and the single tryptophan of the lutropin molecule is located at position 8. The two methionine residues in lutropin-beta are in positions 41 and 42. In addition to COOH-terminal heterogeneity, evidence for internal peptide cleavages was observed.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Carbohydrates / analysis
  • Cattle
  • Chorionic Gonadotropin / analysis
  • Humans
  • Luteinizing Hormone / analysis*
  • Luteinizing Hormone / isolation & purification
  • Peptide Fragments / analysis
  • Sheep
  • Species Specificity
  • Swine
  • Thyrotropin / analysis

Substances

  • Amino Acids
  • Carbohydrates
  • Chorionic Gonadotropin
  • Peptide Fragments
  • Luteinizing Hormone
  • Thyrotropin