Literature DB >> 7282213

Interaction of acid alpha 1-glycoprotein with immunoglobulins.

Z Wróblewski.   

Abstract

1. The acid alpha 1-glycoprotein (alpha 1-AGP) immobilized on Sepharose binds selectively only those immunoglobulins (IgG) of total serum proteins which are eluted either with 0.75 m-NaCl or free alpha 1-AGP. 2. alpha 1-AGP, upon partial enzymatic desialination, loses the ability to bind IgG, and does not acquire the ability to bind other serum proteins. 3. The interaction of alpha 1-AGP with IgG or fragments (Fab')2 depends on pH and ionic strength of the medium. At pH 7.2 and ionic strength of 0.15 alpha 1-AGP forms with IgG soluble complexes in which one molecule of IgG binds six molecules of alpha 1-AGP.

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Year:  1981        PMID: 7282213

Source DB:  PubMed          Journal:  Acta Biochim Pol        ISSN: 0001-527X            Impact factor:   2.149


  1 in total

1.  Concentration-dependent effect of fibrinogen on IgG-specific antigen binding and phagocytosis.

Authors:  Tobias Konrad Boehm; Hakimuddin Sojar; Ernesto Denardin
Journal:  Cell Immunol       Date:  2010-02-24       Impact factor: 4.868

  1 in total

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