Linked Life Data

17010299

Source:http://linkedlifedata.com/resource/pubmed/id/17010299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-10-23
pubmed:abstractText
Site-specific metal-catalyzed oxidation (MCO) was applied to characterize the metal-binding site (MBS) of recombinant human prolactin (hPRL), which belongs to the hematopoietic cytokine family. Copper and ascorbate of various concentrations were used to initiate the oxidation of hPRL, and the oxidation-sensitive motifs were characterized and quantitated by mass spectrometry. Based on the results obtained with 10 microM Cu(2+) and 0.3-2.0mM ascorbate, we propose that the MBS in hPRL is composed of His27, His30, and His173. This result shows the similarity of hPRL to human growth hormone (hGH), a member of the same family as hPRL, where the MBS is composed of His18, His21, and Glu174.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
358
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
208-15
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Characterization of the metal-binding site of human prolactin by site-specific metal-catalyzed oxidation.
pubmed:affiliation
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural