Advanced

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

Manolov, Taras LU ; Forsgren, Arne LU and Riesbeck, Kristian LU (2008) In Journal of Immunological Methods 333. p.180-185
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Immunological Methods
volume
333
pages
180 - 185
publisher
Elsevier
external identifiers
  • pmid:18242635
  • wos:000255734500017
  • scopus:41149095093
ISSN
1872-7905
DOI
10.1016/j.jim.2007.12.012
language
English
LU publication?
yes
id
290d1d58-1ca1-4bcf-8652-bc4c48c98958 (old id 1042331)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18242635?dopt=Abstract
date added to LUP
2008-03-03 14:41:54
date last changed
2017-01-01 07:46:09
@article{290d1d58-1ca1-4bcf-8652-bc4c48c98958,
  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.},
  author       = {Manolov, Taras and Forsgren, Arne and Riesbeck, Kristian},
  issn         = {1872-7905},
  language     = {eng},
  pages        = {180--185},
  publisher    = {Elsevier},
  series       = {Journal of Immunological Methods},
  title        = {Purification of alpha1-antichymotrypsin from human plasma with recombinant M. catarrhalis ubiquitous surface protein A1.},
  url          = {http://dx.doi.org/10.1016/j.jim.2007.12.012},
  volume       = {333},
  year         = {2008},
}