ISOLATION OF A NEUROPEPTIDE CORRESPONDING TO THE N-TERMINAL 27 RESIDUES OF THE PITUITARY ADENYLATE-CYCLASE ACTIVATING POLYPEPTIDE WITH 38 RESIDUES (PACAP38)
ISOLATION OF A NEUROPEPTIDE CORRESPONDING TO THE N-TERMINAL 27 RESIDUES OF THE PITUITARY ADENYLATE-CYCLASE ACTIVATING POLYPEPTIDE WITH 38 RESIDUES (PACAP38)
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DOI:
10.1016/0006-291x(90)92140-u
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发表时间:
1990-07-31
影响因子:
3.1
通讯作者:
ARIMURA, A
中科院分区:
文献类型:
--
作者:
MIYATA, A;JIANG, L;ARIMURA, A
A novel neuropeptide with 38 residues (PACAP38) was isolated from ovine hypothalamic tissues using the pituitary adenylate cyclase activation in rat pituitary cell cultures as a parameter of the biological activity (Miyata et al, Biochem. Biophys. Res. Commun. 164, 567-574, 1989). From the side fractions obtained during the purification of PACAP38, a shorter form peptide with 27 residues corresponding to the N-terminal 27 amino acids of PACAP38 and amidated C-terminus was isolated and named as PACAP27. Synthetic PACAP27 showed a biological activity of adenylate cyclase stimulation comparable to PACAP38. Moreover PACAP27 which shows a considerable homology with vasoactive intestinal polypeptide (VIP) demonstrated a similar vasodepressor activity as VIP, but the adenylate cyclase stimulating activity was about 1000 times greater than VIP.