6533b7d7fe1ef96bd1267967

RESEARCH PRODUCT

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

Manfred P. DierichBeate LandenManfred J. Schmitt

subject

chemistry.chemical_classificationAntigenicityPeriodic acidGeneral MedicineComplement receptorMolecular biologyRaji cellchemistry.chemical_compoundchemistryBiochemistryFactor HPMSFGlycoproteinReceptor

description

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 (α 1 -AT). The activity of α 1 -AT towards-C3 and its fragments was unaffected by heating but it was destroyed by periodic acid. The isolated carbohydrate moiety of α 1 -AT showed the same effect as the intact molecule. Using F(ab) 2 of IgG-anti-α 1 -AT, α 1 -AT could be demonstrated on Raji cells and human erythrocytes. Treatment of these CR + C with IgG-anti-α 1 -AT resulted in a blockade of their C3 receptor activity. The results suggest, that α 1 -AT interacts through its carbohydrate portion with C3 and its fragments and functions as a complement receptor molecule.

yearjournalcountryeditionlanguage
1979-08-01Zeitschrift für Immunitätsforschung: Immunobiology
https://doi.org/10.1016/s0340-904x(79)80071-8