Complement Receptor Analogous Factors in Human Serum: I. Isolation of a Molecule Inhibitory for Complement Dependent Rosette Formation, its Identification as α1-Antitrypsin and its Functional Characterization

Zeitschrift für Immunit?tsforschung: Immunobiology Pub Date : 1979-08-01 DOI:10.1016/S0340-904X(79)80071-8

Manfred P. Dierich , Beate Landen, Manfred Schmitt

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引用次数: 8

Abstract

A glycoprotein was isolated from human plasma which partially inhibited C3 carrying erythrocytes from binding to complement receptor cells (CR⁺C). Based on its physicochemical characteristics and its antigenicity this glycoprotein was identified as aI-antitrypsin (α₁-AT). The activity of α₁-AT towards-C3 and its fragments was unaffected by heating but it was destroyed by periodic acid. The isolated carbohydrate moiety of α₁-AT showed the same effect as the intact molecule. Using F(ab)₂ of IgG-anti-α₁-AT, α₁-AT could be demonstrated on Raji cells and human erythrocytes. Treatment of these CR⁺C with IgG-anti-α₁-AT resulted in a blockade of their C3 receptor activity. The results suggest, that α₁-AT interacts through its carbohydrate portion with C3 and its fragments and functions as a complement receptor molecule.

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人血清中补体受体类似因子:1 .一种补体依赖性玫瑰花形成抑制分子的分离、α1-抗胰蛋白酶鉴定及其功能表征

从人血浆中分离出一种糖蛋白，能部分抑制携带C3的红细胞与补体受体细胞(CR+C)的结合。根据其理化性质和抗原性鉴定该糖蛋白为aI-antitrypsin (α1-AT)。α - 1- at对- c3及其片段的活性不受加热影响，但被周期性酸破坏。α1-AT分离后的碳水化合物部分表现出与完整分子相同的效果。利用igg抗α1-AT的F(ab)2，可以在Raji细胞和人红细胞上证明α1-AT的作用。用IgG-anti-α1-AT治疗这些CR+C可阻断它们的C3受体活性。结果表明，α1-AT通过其碳水化合物部分与C3及其片段相互作用，并作为补体受体分子发挥作用。

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Zeitschrift für Immunit?tsforschung: Immunobiology

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