Partial amino acid sequence analyses of human placental insulin receptor.
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.
Fujita-Yamaguchi
Y
Y
Department of Molecular Genetics, Beckman Research Institute of the City of Hope, Duarte, CA 91010-0269.
Hawke
D H
DH
Shively
J E
JE
Choi
S
S
D000595:Amino Acid Sequence; D004247:DNA / Q000235:genetics; D005260:Female; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy; D011972:Receptor, Insulin / Q000235:genetics / Q000302:isolation & purification; D014357:Trypsin
D010446:Peptide Fragments; D004247:DNA; D011972:Receptor, Insulin; D014357:Trypsin