Purification and characterization of feline ghrelin and its possible role

• Published in: Domestic animal endocrinology Vol. 32; no. 2; pp. 93 - 105
• Main Authors: Ida, Takanori, Miyazato, Mikiya, Naganobu, Kiyokazu, Nakahara, Keiko, Sato, Miho, Lin, Xing-Zi, Kaiya, Hiroyuki, Doi, Kentaro, Noda, Soushi, Kubo, Ayako, Murakami, Noboru, Kangawa, Kenji
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2007
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; Base Sequence; blood; Cat; Cats; chemical structure; chemistry; Chromatography, High Pressure Liquid; Cloning, Molecular; complementary DNA; DNA, Complementary; DNA, Complementary - chemistry; DNA, Complementary - genetics; Enzyme-Linked Immunosorbent Assay; Fasting; fatty acids; feed deprivation; Feeding behavior; genetics; Ghrelin; Growth Hormone; Growth Hormone - blood; hormonal regulation; hormone secretion; isolation & purification; Kinetics; Molecular Sequence Data; nucleotide sequences; Peptide Hormones; Peptide Hormones - chemistry; Peptide Hormones - genetics; Peptide Hormones - isolation & purification; Peptide Hormones - physiology; physiology; purification; somatotropin; Feeding behavior; Growth hormone; Ghrelin; Cat
• ISSN: 0739-7240; 1879-0054
• DOI: 10.1016/j.domaniend.2006.01.002

Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3, has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active...