Literature DB >> 6607264

The use of thiol-disulphide exchange chromatography for the automated isolation of alpha 1-antitrypsin and other plasma proteins with reactive thiol groups.

C B Laurell, I Dahlqvist, U Persson.   

Abstract

A method has been developed for the rapid isolation of alpha 1-antitrypsin and other thiol proteins from plasma by an automated chromatography system. The thiol-proteins are initially bound to matrix-linked activated thiol-compounds by an SH-SS interchange reaction. The mixed disulphides are then reduced in two steps and subfractionated by passage through Blue-Sepharose and AH-Sepharose columns. The rate of the interchange reactions varies with the microenvironment of the reacting thiols. alpha 1-Antitrypsin is recovered with 95% purity in 60% yield within two days from 1 l of plasma.

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Year:  1983        PMID: 6607264     DOI: 10.1016/s0378-4347(00)84755-6

Source DB:  PubMed          Journal:  J Chromatogr


  6 in total

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3.  Binding of Streptococcus pneumoniae endopeptidase O (PepO) to complement component C1q modulates the complement attack and promotes host cell adherence.

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Authors:  Karolina I Smolag; Christine M Mueni; Karin Leandersson; Karin Jirström; Catharina Hagerling; Matthias Mörgelin; Paul N Barlow; Myriam Martin; Anna M Blom
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  6 in total

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