| pubmed-article:15917623 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15917623 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:15917623 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:15917623 | pubmed:dateCreated | 2005-5-26 | lld:pubmed |
| pubmed-article:15917623 | pubmed:abstractText | Ubiquitin-activating enzyme is the archetype for a family of enzymes catalyzing the ATP-coupled activation of ubiquitin and other class 1 ubiquitin-like proteins required for their subsequent conjugation to cellular targets. The general physical and mechanistic features of the E1 family appear well conserved. Formation of an obligatory E1-ubiquitin thiol ester intermediate forms the basis of a one-step covalent purification of the enzyme on ubiquitin-linked affinity columns that has been adapted for the isolation of E1 paralogs. We describe the facile purification of active E1 from outdated human red blood cells in yields (2-4 nmol/U of blood) that make this an attractive alternative to expression of the proteolytically labile recombinant protein. In addition, two stoichiometric activity assays are described that rely on formation of the E1 125I-ubiquitin thiol ester and ubiquitin [2,8-3H]adenylate intermediates. | lld:pubmed |
| pubmed-article:15917623 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15917623 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15917623 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15917623 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15917623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15917623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15917623 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15917623 | pubmed:issn | 1064-3745 | lld:pubmed |
| pubmed-article:15917623 | pubmed:author | pubmed-author:HaasArthur... | lld:pubmed |
| pubmed-article:15917623 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15917623 | pubmed:volume | 301 | lld:pubmed |
| pubmed-article:15917623 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15917623 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15917623 | pubmed:pagination | 23-35 | lld:pubmed |
| pubmed-article:15917623 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15917623 | pubmed:meshHeading | pubmed-meshheading:15917623... | lld:pubmed |
| pubmed-article:15917623 | pubmed:meshHeading | pubmed-meshheading:15917623... | lld:pubmed |
| pubmed-article:15917623 | pubmed:meshHeading | pubmed-meshheading:15917623... | lld:pubmed |
| pubmed-article:15917623 | pubmed:meshHeading | pubmed-meshheading:15917623... | lld:pubmed |
| pubmed-article:15917623 | pubmed:meshHeading | pubmed-meshheading:15917623... | lld:pubmed |
| pubmed-article:15917623 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15917623 | pubmed:articleTitle | Purification of E1 and E1-like enzymes. | lld:pubmed |
| pubmed-article:15917623 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Louisiana State University Health Science Center, New Orleans, USA. | lld:pubmed |
| pubmed-article:15917623 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15917623 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15917623 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
