Purification of alpha1-antichymotrypsin from human plasma with recombinant M. catarrhalis ubiquitous surface protein A1.

Research output: Contribution to journalArticle

Abstract

Alpha 1-antichymotrypsin (ACT) inhibits chymotrypsin-like enzymes, particularly neutrophil cathepsin G. Moreover, ACT in its native form suppresses chemotaxis of neutrophils and decreases neutrophil production of superoxide radicals. We recently showed that Moraxella catarrhalis ubiquitous surface protein (Usp) A1 is able to specifically bind ACT in the context of a novel virulence mechanism. In this study, we report that recombinant UspA1(557-704) coupled to CNBr-Sepharose can be used in a simple one-step purification of ACT from human plasma. UspA1(557-704)-purified ACT remains intact and active as shown by binding to M. catarrhalis and a chymotrypsin inhibition assay. The novel method for ACT isolation from plasma has important advantages in simplicity and time as compared to conventional methods.

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Subject classification (UKÄ) – MANDATORY

  • Immunology in the medical area
Original languageEnglish
Pages (from-to)180-185
JournalJournal of Immunological Methods
Volume333
Publication statusPublished - 2008
Publication categoryResearch
Peer-reviewedYes

Related research output

Taras Manolov, 2009, Department of Laboratory Medicine, Lund University.

Research output: ThesisDoctoral Thesis (compilation)

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