Linked Life Data

6706936

Source:http://linkedlifedata.com/resource/pubmed/id/6706936

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-5-11
pubmed:abstractText
HPRTMunich is a mutant form of human hypoxanthine-guanine phosphoribosyltransferase that was isolated from a patient who presented with gout and a partial deficiency of enzyme activity. Profound abnormalities in the catalytic function of HPRTMunich are responsible for the deficiency of enzyme activity in vivo. Tryptic peptides of HPRTMunich were mapped by reverse phase high pressure liquid chromatography in an attempt to define the precise abnormality in its primary structure. Sequence analysis of aberrant peptides localized the structural alteration in HPRTMunich to residue 103. Several additional findings suggest that the mutation in this variant is most likely a serine to arginine substitution at residue 103. This amino acid substitution lies within the putative hypoxanthine-binding site of human hypoxanthine-guanine phosphoribosyltransferase possibly explaining its selective effect on intrinsic enzyme activity and binding of hypoxanthine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-30
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't