Matsas R, Rattray M, Kenny A J, Turner A J
Biochem J. 1985 Jun 1;228(2):487-92. doi: 10.1042/bj2280487.
Synaptic membrane preparations from human striatum and human diencephalon were shown to contain a phosphoramidon-sensitive metalloendopeptidase that appeared identical with endopeptidase-24.11. The activity of endopeptidase-24.11 was determined with an enzymic assay employing [D-Ala2,Leu5]enkephalin as substrate, and its distribution in human brain was similar to that in pig brain, with the striatum containing the highest levels. The choroid plexus and pons also contained substantial activity. A good correlation (r = 0.97) was obtained for the distribution of the endopeptidase in pig brain and pituitary by the enzymic assay and by an immunoradiometric assay specific for pig endopeptidase-24.11. Synaptic membrane preparations from human striatum and diencephalon hydrolysed substance P at the same sites as did preparations of pig striatal synaptic membranes, and hydrolysis was substantially abolished by phosphoramidon. These results suggest that endopeptidase-24.11 is the principal enzyme hydrolysing substance P in human synaptic membrane preparations.
来自人类纹状体和间脑的突触膜制剂显示含有一种对磷酰胺脒敏感的金属内肽酶,该酶似乎与内肽酶-24.11相同。以内啡肽[D-Ala2,Leu5]为底物,通过酶法测定内肽酶-24.11的活性,其在人类大脑中的分布与猪脑相似,纹状体中的含量最高。脉络丛和脑桥也含有大量活性。通过酶法测定以及针对猪内肽酶-24.11的免疫放射测定法,在猪脑和垂体中内肽酶的分布获得了良好的相关性(r = 0.97)。来自人类纹状体和间脑的突触膜制剂与猪纹状体突触膜制剂一样,在相同位点水解P物质,并且磷酰胺脒可大大消除水解作用。这些结果表明,内肽酶-24.11是人类突触膜制剂中水解P物质的主要酶。