Partial amino acid sequence analyses of human placental insulin receptor

Protein Seq Data Anal. 1987;1(1):3-6.

Abstract

Tryptic peptides were isolated from human insulin receptor (1.8 nmol) by sequential reverse-phase HPLC on SynChropak RP-C8 and Vydac C-18. Nearly 20 peptides were analyzed for amino acid composition, which revealed that the yield of tryptic peptides averaged 300 pmol. By gas-phase microsequencing five peptides were sequenced. N-acetylglucosamine was found in two peptides. These data are compared with the amino acid sequence of the insulin receptor deduced from cloned cDNA encoding for human insulin receptor.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • DNA / genetics
  • Female
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • Placenta / analysis*
  • Pregnancy
  • Receptor, Insulin* / genetics
  • Receptor, Insulin* / isolation & purification
  • Trypsin

Substances

  • Peptide Fragments
  • DNA
  • Receptor, Insulin
  • Trypsin