One-step purification of recombinant human amelogenin and use of amelogenin as a fusion partner.
Svensson Bonde, Johan LU
and Bülow, Leif
LU
(2012)
In PLoS ONE
7(3).
- Abstract
- Amelogenin is an extracellular protein first identified as a matrix component important for formation of dental enamel during tooth development. Lately, amelogenin has also been found to have positive effects on clinical important areas, such as treatment of periodontal defects, wound healing, and bone regeneration. Here we present a simple method for purification of recombinant human amelogenin expressed in Escherichia coli, based on the solubility properties of amelogenin. The method combines cell lysis with recovery/purification of the protein and generates a >95% pure amelogenin in one step using intact harvested cells as starting material. By using amelogenin as a fusion partner we could further demonstrate that the same method... (More)
- Amelogenin is an extracellular protein first identified as a matrix component important for formation of dental enamel during tooth development. Lately, amelogenin has also been found to have positive effects on clinical important areas, such as treatment of periodontal defects, wound healing, and bone regeneration. Here we present a simple method for purification of recombinant human amelogenin expressed in Escherichia coli, based on the solubility properties of amelogenin. The method combines cell lysis with recovery/purification of the protein and generates a >95% pure amelogenin in one step using intact harvested cells as starting material. By using amelogenin as a fusion partner we could further demonstrate that the same method also be can explored to purify other target proteins/peptides in an effective manner. For instance, a fusion between the clinically used protein PTH (parathyroid hormone) and amelogenin was successfully expressed and purified, and the amelogenin part could be removed from PTH by using a site-specific protease. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2431529
- author
- Svensson Bonde, Johan
LU
and Bülow, Leif
LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 7
- issue
- 3
- article number
- e33269
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- wos:000303836500022
- pmid:22442680
- scopus:84858606856
- pmid:22442680
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0033269
- language
- English
- LU publication?
- yes
- id
- fb2aec9b-41bc-4648-b7db-dd0ed64ced9a (old id 2431529)
- date added to LUP
- 2016-04-01 14:18:48
- date last changed
- 2023-11-13 05:51:07
@article{fb2aec9b-41bc-4648-b7db-dd0ed64ced9a,
abstract = {{Amelogenin is an extracellular protein first identified as a matrix component important for formation of dental enamel during tooth development. Lately, amelogenin has also been found to have positive effects on clinical important areas, such as treatment of periodontal defects, wound healing, and bone regeneration. Here we present a simple method for purification of recombinant human amelogenin expressed in Escherichia coli, based on the solubility properties of amelogenin. The method combines cell lysis with recovery/purification of the protein and generates a >95% pure amelogenin in one step using intact harvested cells as starting material. By using amelogenin as a fusion partner we could further demonstrate that the same method also be can explored to purify other target proteins/peptides in an effective manner. For instance, a fusion between the clinically used protein PTH (parathyroid hormone) and amelogenin was successfully expressed and purified, and the amelogenin part could be removed from PTH by using a site-specific protease.}},
author = {{Svensson Bonde, Johan and Bülow, Leif}},
issn = {{1932-6203}},
language = {{eng}},
number = {{3}},
publisher = {{Public Library of Science (PLoS)}},
series = {{PLoS ONE}},
title = {{One-step purification of recombinant human amelogenin and use of amelogenin as a fusion partner.}},
url = {{http://dx.doi.org/10.1371/journal.pone.0033269}},
doi = {{10.1371/journal.pone.0033269}},
volume = {{7}},
year = {{2012}},
}