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大鼠的α-1急性期球蛋白。分离及某些特性

Alpha-1 acute-phase globulins of rats. Isolation and some properties.

作者信息

Gordon A H, Louis L N

出版信息

Biochem J. 1969 Jul;113(3):481-8. doi: 10.1042/bj1130481.

Abstract
  1. A method is described for the isolation of certain of the alpha(1)-globulins of rat plasma that are known to increase in concentration after tissue damage (acute-phase globulins). 2. Although apparently homogeneous when examined by disc electrophoresis at pH9, these proteins could be subdivided further by isoelectric fractionation. 3. Treatment with neuraminidase removed approx. 60% of the sialic acid originally present in these proteins and gave almost completely homogeneous material of decreased mobility when examined by disc electrophoresis in polyacrylamide gel. When subjected to immunoelectrophoresis this material gave a single arc. 4. The homogeneity of the isolated materials was examined by ultracentrifugation. The single peak thus found is consistent with molecular weights of 45000-46000. 5. The isolated materials were shown to be glycoproteins containing approx. 15% of carbohydrate, and to have isoelectric points in the range pH4.4-4.8.
摘要
  1. 本文描述了一种从大鼠血浆中分离某些α(1)-球蛋白的方法,这些球蛋白在组织损伤后(急性期球蛋白)浓度会升高。2. 虽然在pH9的圆盘电泳中检测时这些蛋白质看起来是均一的,但通过等电分级可以进一步细分。3. 用神经氨酸酶处理可去除这些蛋白质中约60%的唾液酸,当在聚丙烯酰胺凝胶中进行圆盘电泳检测时,得到的物质迁移率降低且几乎完全均一。对该物质进行免疫电泳时,出现单一弧线。4. 通过超速离心检测分离出的物质的均一性。由此发现的单峰与分子量45000 - 46000一致。5. 分离出的物质被证明是糖蛋白,含有约15%的碳水化合物,且等电点在pH4.4 - 4.8范围内。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b14b/1184690/01bfe97493ba/biochemj00699-0034-a.jpg

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