Kelly P T, McGuinness T L, Greengard P
Proc Natl Acad Sci U S A. 1984 Feb;81(3):945-9. doi: 10.1073/pnas.81.3.945.
Polypeptides of Mr 50,000 and 60,000 in isolated synaptic junctions have been compared to polypeptides of corresponding molecular weight in Ca2+/calmodulin-dependent protein kinase II. The polypeptides of corresponding molecular weight from the two preparations were shown by several criteria to be indistinguishable. These criteria included 125I-labeled tryptic/chymotryptic peptide patterns, 32P-labeled proteolytic peptide maps, and crossreactivity on immunoblots using polyclonal and monoclonal antibodies. Furthermore, studies examining the phosphorylation of substrate proteins, by the endogenous synaptic junction kinase and by Ca2+/calmodulin-dependent protein kinase II, indicated that the two enzymes have similar substrate specificities. Since the Mr 50,000 polypeptide present in synaptic junctions is known to be the major postsynaptic density protein, the present results indicate that the major postsynaptic density protein is a component of Ca2+/calmodulin-dependent protein kinase II.
已将分离出的突触连接处分子量为50,000和60,000的多肽与钙/钙调蛋白依赖性蛋白激酶II中相应分子量的多肽进行了比较。通过若干标准表明,这两种制剂中相应分子量的多肽无法区分。这些标准包括125I标记的胰蛋白酶/胰凝乳蛋白酶肽图谱、32P标记的蛋白水解肽图谱,以及使用多克隆和单克隆抗体在免疫印迹上的交叉反应性。此外,对内源性突触连接激酶和钙/钙调蛋白依赖性蛋白激酶II对底物蛋白磷酸化的研究表明,这两种酶具有相似的底物特异性。由于已知突触连接处存在的分子量为50,000的多肽是主要的突触后致密蛋白,目前的结果表明,主要的突触后致密蛋白是钙/钙调蛋白依赖性蛋白激酶II的一个组成部分。