Sandin J, Tan-No K, Kasakov L, Nylander I, Winter A, Silberring J, Terenius L
Department of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.
Peptides. 1997;18(7):949-56. doi: 10.1016/s0196-9781(97)00025-9.
To map the proteolytic enzymes metabolizing dynorphins in brain structures, size-exclusion chromatography linked to electrospray ionization mass spectrometry was used. Enzymes extracted from rat hippocampus, striatum, and substantia nigra were tested for their capability of converting dynorphin-related peptides. Dynorphin A was the most resistant to proteolytic conversion, whereas Big dynorphin and dynorphin B-29 were slowly converted to dynorphin A and dynorphins A and B, respectively. Dynorphin B and alpha-neoendorphin were the least resistant. Dynorphin B was rapidly converted to Leu-enkephalin in the striatum and hippocampus but to Leu-enkephalin-Arg6 in the substantia nigra. alpha-Neoendorphin was converted to Leu-enkephalin in all tissues investigated.
为了绘制在脑结构中代谢强啡肽的蛋白水解酶图谱,采用了与电喷雾电离质谱联用的尺寸排阻色谱法。对从大鼠海马体、纹状体和黑质中提取的酶进行了转化强啡肽相关肽能力的测试。强啡肽A对蛋白水解转化最具抗性,而大强啡肽和强啡肽B - 29分别缓慢转化为强啡肽A以及强啡肽A和B。强啡肽B和α-新内啡肽抗性最低。强啡肽B在纹状体和海马体中迅速转化为亮氨酸脑啡肽,但在黑质中转化为亮氨酸脑啡肽-精氨酸6。α-新内啡肽在所有研究的组织中都转化为亮氨酸脑啡肽。