Takahashi M, Moriguchi S, Yoshikawa M, Sasaki R
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Biochem Mol Biol Int. 1994 Aug;33(6):1151-8.
A novel bioactive peptide was isolated from the tryptic digest of rice soluble protein based on ileum-contracting and anti-opioid activities in the isolated guinea pig ileum. The structure of the peptide was Gly-Tyr-Pro-Met-Tyr-Pro-Leu-Pro-Arg, and it was named oryzatensin. Oryzatensin showed a biphasic ileum-contraction, which was characterized by a rapid contraction followed by a slower one. The latter was mediated by the cholinergic nervous system because it was inhibited by tetrodotoxin and atropine. Although oryzatensin showed weak affinity for mu-opioid receptors, the apparent anti-opioid activity seemed to be associated with the slower contraction. On the other hand, oryzatensin showed phagocytosis-promoting activity for human polymorphonuclear leukocytes and augmented the production of superoxide anion by human peripheral leukocytes.
基于对豚鼠离体回肠的回肠收缩和抗阿片样物质活性，从水稻可溶性蛋白的胰蛋白酶消化物中分离出一种新型生物活性肽。该肽的结构为甘氨酸-酪氨酸-脯氨酸-甲硫氨酸-酪氨酸-脯氨酸-亮氨酸-脯氨酸-精氨酸，命名为稻紧张素。稻紧张素表现出双相回肠收缩，其特征是先快速收缩，随后是较慢的收缩。后者由胆碱能神经系统介导，因为它受到河豚毒素和阿托品的抑制。尽管稻紧张素对μ-阿片样物质受体表现出较弱的亲和力，但其明显的抗阿片样物质活性似乎与较慢的收缩有关。另一方面，稻紧张素对人多形核白细胞表现出促进吞噬作用，并增强人外周白细胞超氧阴离子的产生。
