Kitamura K, Kangawa K, Tanaka K, Matsuo H
First Department of Internal Medicine, Miyazaki Medical College, Japan.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):1164-71. doi: 10.1016/0006-291x(90)92018-u.
In the present purification of low molecular weight fractions (Mr: 2000-4000) containing basic peptides, twenty nmol of novel calmodulin binding peptide, possessing a potent affinity for calmodulin, was isolated from 18 kg of porcine brain. By analysis with gas phase sequencer, the sequence was determined to be APAEDLARYYSALRHYINLITRQRY. Carboxy terminus of the peptide was determined to be Tyr-NH2. The peptide was a carboxy terminal pentacosanepeptide of neuropeptide Y and was termed NPY-25. NPY-25 competitively inhibited the activation of cAMP-phosphodiesterase through CaM binding in a Ca++ dependent fashion, but did not inhibit the basal activity of cAMP phosphodiesterase. NPY-25 elicited a more potent activity than did neuropeptide Y. IC50 values of NPY-25 and Neuropeptide Y were 0.06 microM and 0.54 microM respectively.
在目前对含有碱性肽的低分子量组分（分子量：2000 - 4000）的纯化过程中，从18千克猪脑中分离出了20纳摩尔对钙调蛋白具有强亲和力的新型钙调蛋白结合肽。通过气相测序仪分析，确定其序列为APAEDLARYYSALRHYINLITRQRY。该肽的羧基末端确定为Tyr - NH2。该肽是神经肽Y的羧基末端二十五肽，被命名为NPY - 25。NPY - 25通过依赖Ca++的方式与钙调蛋白结合竞争性抑制cAMP - 磷酸二酯酶的激活，但不抑制cAMP磷酸二酯酶的基础活性。NPY - 25比神经肽Y具有更强的活性。NPY - 25和神经肽Y的IC50值分别为0.06微摩尔和0.54微摩尔。
