Schousboe I
Biochim Biophys Acta. 1979 Aug 28;579(2):396-408. doi: 10.1016/0005-2795(79)90067-9.
A serum protein named agglutinin is able to induce mitochondria to agglutinate. The protein has been purified from human serum by chromatography on DE-52. Sephadex G-200 and immunoglobulin-Sepharose 4B columns. Agglutinin is a glycoprotein that migrates electrophoretically as a gamma-globulin. Its molecular weight was determined to be 50,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monospecific antiserum prepared against the agglutinin was found to be identical with anti-beta 2-glycoprotein I and agglutinating activity could be adsorbed on anti-beta 2-glycoprotein I-Sepharose 4B columns. Thus, the agglutinin has been identified as beta 2-glycoprotein I. The reaction between mitochondria and agglutinin shows positive cooperativity, which is independent on the stage of purification of agglutinin. The agglutinating activity could be diminished (inhibited) by acidic non-soluble lipids such as oleic acid, phosphatidic acid, phosphatidyl serine and phosphatidyl inositol.
一种名为凝集素的血清蛋白能够诱导线粒体凝集。该蛋白已通过在DE - 52、Sephadex G - 200和免疫球蛋白 - Sepharose 4B柱上进行层析从人血清中纯化出来。凝集素是一种糖蛋白，在电泳时作为γ - 球蛋白迁移。在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳上测定其分子量为50,000。发现针对凝集素制备的单特异性抗血清与抗β2 - 糖蛋白I相同，并且凝集活性可被吸附在抗β2 - 糖蛋白I - Sepharose 4B柱上。因此，凝集素已被鉴定为β2 - 糖蛋白I。线粒体与凝集素之间的反应表现出正协同性，这与凝集素的纯化阶段无关。凝集活性可被酸性不溶性脂质如油酸、磷脂酸、磷脂酰丝氨酸和磷脂酰肌醇降低（抑制）。
