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pro vyhledávání: '"621"'
Autor:
Noritoshi Kawate, K.M.J. Menon
Publikováno v:
Journal of Biological Chemistry. 269:30651-30658
We have examined whether the two cysteine residues (621 and 622) of the carboxyl-terminal cytoplasmic domain of the rat luteinizing hormone (LH/hCG) receptor are potential sites for palmitoylation. The full-length LH/hCG receptor cDNA was cloned into
Publikováno v:
Journal of Biological Chemistry. 273:11150-11157
The extracellular domain of the human epidermal growth factor receptor (sEGFR) consists of 621 amino acid residues, including 50 cysteines. The connections of the 25 disulfide bonds in the recombinant sEGFR protein, obtained from Chinese hamster ovar