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血清淀粉样蛋白A(SAA)与自身及血清白蛋白的蛋白相互作用。

Serum amyloid A (SAA) protein-interaction with itself and serum albumin.

作者信息

Rosenthal C J, Franklin E C

出版信息

J Immunol. 1977 Aug;119(2):630-4.

PMID:301900
Abstract

Serum amyloid A (SAA) protein is a 12,000 dalton protein that exists in serum under physiologic conditions as an 85,000 dalton complex and under certain conditions, as a 170,000 dalton component. To study the reason for this finding, the behavior of 125I-SAA was studied in the presence of cold SAA and several serum proteins. SAA caused a shift of some of the radioactivity to the region of albumin. Addition of normal human serum or albumin caused a shift of a significant fraction of the radioactivity to a peak eluting slightly ahead of albumin (80.000 daltons). This interaction could be blocked by the addition of cold SAA. No shift was noted when IgG or Bence Jones proteins were added. Thus, it appears that low molecular SAA protein has a tendency to aggregate with itself and to bind to albumin but not to human IgG or Bence Jones proteins.

摘要

血清淀粉样蛋白A(SAA)是一种分子量为12,000道尔顿的蛋白质,在生理条件下以85,000道尔顿的复合物形式存在于血清中,在某些条件下则以170,000道尔顿的成分存在。为了研究这一发现的原因,我们在冷SAA和几种血清蛋白存在的情况下研究了125I-SAA的行为。SAA导致部分放射性转移到白蛋白区域。添加正常人血清或白蛋白会使相当一部分放射性转移到一个略先于白蛋白洗脱的峰(80,000道尔顿)。这种相互作用可通过添加冷SAA来阻断。添加IgG或本-周蛋白时未观察到转移。因此,似乎低分子SAA蛋白有自身聚集并与白蛋白结合的倾向,但不与人类IgG或本-周蛋白结合。

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