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Partial amino acid sequence analyses of human placental insulin receptor
Y Fujita-Yamaguchi1, D H Hawke, J E Shively
1Department of Molecular Genetics, Beckman Research Institute of the City of Hope, Duarte, CA 91010-0269.
Protein Sequences & Data Analysis
|January 1, 1987
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.