Identification of amidicin: a novel peptide with C-terminal amide structure isolated from porcine cardiac atrium.
Using a novel method employing a V8 protease digestion coupled with ethyl acetate extraction, we have purified a peptide with C-terminal amide structure from porcine cardiac atrium. The peptide was determined to be Ala-Val-Leu-Gly-Leu-CONH2. According to the sequence, we have raised an antibody and established the radioimmunoassay. Using this radioimmunoassay, we have isolated a novel 14 amino acid peptide where C-terminus was amidated. This peptide was termed amidicin. Amidicin is widely distributed in porcine tissue and is especially abundant in pituitary gland, cardiac ventricle, and spleen.
Ishiyama
Yuichiro
Y
First Department of Internal Medicine, Miyazaki Medical College, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.
Kitamura
Kazuo
K
Eto
Tanenao
T
D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D006325:Heart Atria / Q000737:chemistry*; D010455:Peptides / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification*; D013552:Swine; D014018:Tissue Distribution
D000577:Amides; D010455:Peptides