| pubmed-article:16298141 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C0262950 | lld:lifeskim |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:16298141 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:16298141 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16298141 | pubmed:dateCreated | 2006-4-3 | lld:pubmed |
| pubmed-article:16298141 | pubmed:abstractText | Homodimeric bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta superfamily that has been used for bone grafting. We were interested in exploring the functions of BMP-2 in other disease areas and focused on expressing and purifying active BMP-2 proteins. We have developed a new approach which involves using FoldIt refolding buffer to refold BMP-2 followed by a heparin affinity column to separate correctly folded dimer from monomer. A high yield of 29.4 mg BMP-2 dimer per gram cell wet weight was achieved. The purified BMP-2 dimer was shown to possess the same level of activity as BMP-2 from CHO cells as tested by the induction of alkaline phosphatase activity in C2C12 cells. This approach has potential application in refolding and purifying other homodimeric proteins. | lld:pubmed |
| pubmed-article:16298141 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16298141 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16298141 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16298141 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16298141 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16298141 | pubmed:issn | 1046-5928 | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:Wong-StaalFlo... | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:TruongLynnL | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:PhillipsAndre... | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:MaHongwenH | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:LongShinongS | lld:pubmed |
| pubmed-article:16298141 | pubmed:author | pubmed-author:BennettKrista... | lld:pubmed |
| pubmed-article:16298141 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16298141 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:16298141 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16298141 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16298141 | pubmed:pagination | 374-8 | lld:pubmed |
| pubmed-article:16298141 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:meshHeading | pubmed-meshheading:16298141... | lld:pubmed |
| pubmed-article:16298141 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16298141 | pubmed:articleTitle | Expression, purification, and renaturation of bone morphogenetic protein-2 from Escherichia coli. | lld:pubmed |
| pubmed-article:16298141 | pubmed:affiliation | Immusol, Inc., 10790 Roselle Street, San diego, CA 92121, USA. long@immusol.com | lld:pubmed |
| pubmed-article:16298141 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16298141 | lld:pubmed |
