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:
https://lup.lub.lu.se/record/1042331
- author
- Manolov, Taras
LU
; Forsgren, Arne
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2008
- 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
- 2016-04-04 09:17:27
- date last changed
- 2022-01-29 17:11:32
@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}},
doi = {{10.1016/j.jim.2007.12.012}},
volume = {{333}},
year = {{2008}},
}