Veiby O P, Sletten K, Husby G, Nordstoga K
Department of Biochemistry, University of Oslo, Norway.
Scand J Immunol. 1992 Jan;35(1):63-9. doi: 10.1111/j.1365-3083.1992.tb02834.x.
The elution pattern obtained when amyloid fibrils from amyloid-laden bovine kidneys were subjected to gel filtration under dissociating conditions revealed a larger amount of non-AA material (eluting between the void volume and protein AA) than usually seen in other species. SDS-PAGE of this non-AA fraction yielded several Coomassie blue stained bands. The most distinctive ones gave estimated molecular masses of 15 kDa, 18 kDa, 33 kDa and 43 kDa. These molecular species were electroblotted onto PVDF membranes, and were further characterized by amino acid composition analyses, cyanogen bromide cleavage and N-terminal analyses. The results revealed that the intermediate 'non-AA' fraction consisted of histones H2B, H3 and H4 in addition to protein AA also found in this fraction.
当对来自富含淀粉样蛋白的牛肾脏的淀粉样纤维在解离条件下进行凝胶过滤时，所获得的洗脱模式显示，与其他物种中通常所见相比，有大量的非AA物质（在空体积和蛋白质AA之间洗脱）。该非AA级分的SDS-PAGE产生了几条考马斯亮蓝染色带。最明显的条带估计分子量为15 kDa、18 kDa、33 kDa和43 kDa。这些分子种类被电印迹到PVDF膜上，并通过氨基酸组成分析、溴化氰裂解和N端分析进行进一步表征。结果表明，中间的“非AA”级分除了该级分中也发现的蛋白质AA外，还由组蛋白H2B、H3和H4组成。
