Capaldi D, Rosario R, Esteban E T, Bahr B A
Center for the Neurobiology of Learning and Memory, University of California, Irvine 92697, USA.
Neurosci Res. 1997 Jul;28(3):275-9. doi: 10.1016/s0168-0102(97)00049-7.
A 27-kDa protein from adult rat brain synaptosomes was purified by matrix-affinity chromatography. The matrix receptor interacted with the Arg-Gly-Asp-Ser sequence recognized by integrin-type adhesion molecules, and was labeled by integrin antibodies. Levels of the 27-kDa species in brain membranes were unaffected by proteolysis, however, conventional integrin subunits exhibited robust degradation. This unique resistance to proteolysis may allow the new matrix receptor to contribute to the stability of synaptic contacts.
通过基质亲和层析法从成年大鼠脑突触体中纯化出一种27 kDa的蛋白质。该基质受体与整合素型黏附分子识别的精氨酸-甘氨酸-天冬氨酸-丝氨酸序列相互作用，并被整合素抗体标记。然而，脑膜中27 kDa蛋白的水平不受蛋白水解的影响，而传统的整合素亚基则表现出强烈的降解。这种对蛋白水解的独特抗性可能使新的基质受体有助于突触接触的稳定性。
