Degradation of neuropeptides by calcium-activated neutral protease.
Degradation of neuropeptides by calcium-activated neutral protease.
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钙激活中性蛋白酶降解神经肽。
DOI：
10.1093/oxfordjournals.jbchem.a134564
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发表时间：
1983
影响因子：
2.7
通讯作者：
K. Takahashi
中科院分区：
文献类型：
--
作者：
T. Hirao;K. Hara;K. Takahashi
以不同的神经肽为底物，研究了猴心肌钙激活中性蛋白酶(CANP)的底物特异性。该酶需要mM级钙离子才能激活，并具有脑啡肽酶活性，在1Tyr-2Gly和3Gly-4Phe键上水解亮氨酸-脑啡肽。此外，它还表现出特别是在α-和β-新内啡肽和强啡肽(1-13)中的成对碱性氨基酸残基附近的键被切割的趋势，而不能水解P物质。
The substrate specificity of calcium-activated neutral protease (CANP) from monkey cardiac muscle was examined with various neuropeptides as substrates. The enzyme required mM order calcium ions for activation and had an enkephalinase activity, hydrolyzing Leu-enkephalin at the 1Tyr-2Gly and 3Gly-4Phe bonds. Furthermore, it showed the tendency to cleave especially the bonds around the paired basic amino acid residues in alpha- and beta-neoendorphins and dynorphin(1-13), while it could not hydrolyze substance P.