Hallak M E, Barra H S, Caputto R
J Neurochem. 1985 Mar;44(3):665-9. doi: 10.1111/j.1471-4159.1985.tb12865.x.
Many of the cytosolic proteins of the rat brain appear to have the capacity to incorporate L-[14C]arginine posttranslationally. Scanning of the electrophoretic pattern of the labeled proteins showed two main radioactive peaks: peak A, found in the region of proteins of MW above 200 kD, and peak B, found in the region of 33 kD. The ratio of peaks A/B tends to decrease with the age of the rats. Another zone of radioactivity has an apparent MW similar to that of albumin (approximately 66 kD). No differences were found between the effects of ionic strength and of inhibitors on the arginyl transferase of brain and those described for the transferases of other organs.
大鼠脑内的许多胞质蛋白似乎具有在翻译后掺入L-[14C]精氨酸的能力。对标记蛋白的电泳图谱进行扫描显示出两个主要的放射性峰:峰A,出现在分子量高于200 kD的蛋白区域;峰B,出现在33 kD区域。峰A/峰B的比值往往会随着大鼠年龄的增长而降低。另一个放射性区域的表观分子量与白蛋白的相似(约66 kD)。未发现离子强度和抑制剂对脑精氨酰转移酶的作用与对其他器官转移酶所描述的作用之间存在差异。