Nyberg F, Silberring J
Department of Pharmacology, University of Uppsala, Sweden.
Prog Clin Biol Res. 1990;328:261-5.
This study describes three different endopeptidases in human spinal cord with high affinity for the dynorphins. The enzymes, with strict specificity towards paired basic residues, release Leu-enkephalin and its C-terminal extensions - Arg6 and -Arg6 -Arg7 from the substrate peptides. They differ with regard to molecular size, charge properties, and inhibitory profile. Two of the enzymes show optimal activity at neutral pH, whereas the third enzyme has its activity optimum at pH 5.6. They are all suggested to be of importance for the formation of Leu-enkephalin from prodynorphin.
本研究描述了人脊髓中对强啡肽具有高亲和力的三种不同内肽酶。这些酶对成对碱性残基具有严格的特异性，可从底物肽中释放亮脑啡肽及其C末端延伸片段——-Arg6和-Arg6 -Arg7。它们在分子大小、电荷性质和抑制谱方面存在差异。其中两种酶在中性pH下表现出最佳活性，而第三种酶在pH 5.6时活性最佳。它们都被认为对从强啡肽原形成亮脑啡肽具有重要作用。
