Chicken ghrelin: purification, cDNA cloning, and biological activity.

@article{Kaiya2002ChickenGP,
  title={Chicken ghrelin: purification, cDNA cloning, and biological activity.},
  author={Hiroyuki Kaiya and Serge van der Geyten and Masayasu Kojima and Hiroshi Hosoda and Yasuo Kitajima and Masaru Matsumoto and Sofie M. E. Geelissen and Veerle M. Darras and Kenji Kangawa},
  journal={Endocrinology},
  year={2002},
  volume={143 9},
  pages={3454-63}
}
In this study, we report the purification, cDNA cloning, and characterization of the novel growth hormone-releasing peptide, ghrelin, in the chicken (Gallus gallus). Chicken ghrelin is composed of 26 amino acids (GSSFLSPTYKNIQQQKDTRKPTARLH) and possesses 54% sequence identity with human ghrelin. The serine residue at position 3 (Ser(3)) is conserved between the chicken and mammalian species, as its acylation by either n-octanoic or n-decanoic acid. Chicken ghrelin mRNA is predominantly… CONTINUE READING
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