论文部分内容阅读
Adrenomedullin (AdM), consisting of 52 amino acids, is a newly isolated pepotide from human pheochromocytoma. With hypotensive activity in normotensive rat, AdM was thought to be a newly discovered peptide in the regulation of blood pressure. To investigate the biological functions and mechanisms of AdM, we synthesized AdM by the method of solid-phase in a Beckman 990B automatic peptide synthesizer. Synthesized AdM was cyclized and purified with final purity >98%. Its structure was same as AdM isolated from phechromocvtoma.
Adrenomedullin (AdM), consisting of 52 amino acids, is a newly isolated pepotide from human pheochromocytoma. With hypotensive activity in normotensive rat, AdM was thought to be newly discovered peptide in the regulation of blood pressure. To investigate the biological functions and mechanisms of AdM, we synthesized AdM by the method of solid-phase in a Beckman 990B automatic peptide synthesizer. Synthesized AdM was cyclized and purified with final purity> 98%. Its structure was the same as AdM isolated from phechromocvtoma.