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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
PLoS ONE
volume
7
issue
3
publisher
Public Library of Science
external identifiers
  • wos:000303836500022
  • pmid:22442680
  • scopus:84858606856
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
2012-04-12 14:46:45
date last changed
2017-11-19 03:55:12
@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.},
  articleno    = {e33269},
  author       = {Svensson Bonde, Johan and Bülow, Leif},
  issn         = {1932-6203},
  language     = {eng},
  number       = {3},
  publisher    = {Public Library of Science},
  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},
  volume       = {7},
  year         = {2012},
}