Linked Life Data

8605025

Source:http://linkedlifedata.com/resource/pubmed/id/8605025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-5-15
pubmed:databankReference
pubmed:abstractText
Histamine N-methyltransferase (HNMT) catalyzes the N(tau)-methylation of histamine. The level of HNMT activity in human red blood cells is controlled by a common genetic polymorphism. We previously cloned and expressed a cDNA for human kidney HNMT, and we have now determined the structural organization of the human HNMT gene as a step toward studies of the genetic regulation of levels of HNMT activity in human tissue. Structural characterization of the HNMT gene was performed by use of a polymerase chain reaction (PCR)-based strategy. The gene was approximately 34 kb in length and contained 6 exons. All exon-intron splice junction sequences conformed to the "GT-AG" rule. The longest transcript isolated after 5'-rapid amplification of cDNA ends indicated that transcription initiation occurred 252 nucleotides 5'-upstream from the cDNA translation initiation codon. HNMT mapped to human chromosome 2. Structural characterization of the gene for HNMT will make it possible to study molecular genetic mechanisms involved in the regulation of this important enzyme in humans.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
219
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
548-54
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Human histamine N-methyltransferase gene: structural characterization and chromosomal location.
pubmed:affiliation
Department of Pharmacology, Mayo Medical School, Mayo Foundation, Rochester, Minnesota 55905, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.