화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.293, No.2, 741-746, 2002
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. (C) 2002 Elsevier Science (USA). All rights reserved.