Linked Life Data

15917623

Source:http://linkedlifedata.com/resource/pubmed/id/15917623

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-5-26
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 We describe the facile purification of active E1 from outdated human red blood cells in yields (2-4 nmol/U of blood) that make this an attractive alternative to expression of the proteolytically labile recombinant protein.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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
301
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Purification of E1 and E1-like enzymes.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Louisiana State University Health Science Center, New Orleans, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural