Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2000-10-10
pubmed:databankReference
pubmed:abstractText
Heat lability of the mouse hepatic microsomal epoxide hydrolase 1 enzyme-specific activity (EC 3.3.2.3) is greater for the A/J than the C57BL/6J strain. Analysis of the microsomal epoxide hydrolase 1 cDNA coding sequences shows the C57BL/6J and A/J strains to differ in a single base, a C to T transition at position 1012 from the ATG. This change would predict a substitution of an Arg for a Cys at codon 338. Lyman et al. (J. Biol. Chem 255:8650, 1980) studied 26 inbred mouse strains and assigned each strain to one of two groups based upon functional criteria that included heat lability and pH optima for microsomal epoxide hydrolase 1. The heat-labile strains including A/J were denoted with the Ephx1(d) allele, whereas C57BL/6J and other members of the heat-stable strains were denoted with the Ephx1(b) allele. We examined those same inbred mouse strains and found complete concordance between the assignment of microsomal epoxide hydrolase 1 allele superscript "b" or "d" and the wild-type and C1012T polymorphism respectively (Fisher's Exact Test, two-sided p < 0.0001). These data suggest that mouse hepatic microsomal epoxide hydrolase 1 heat lability is associated with the presence of a Cys at residue 338. Genomic samples from the available AXB and BXA recombinant inbred strains were allelotyped for the SNP identified in the Ephx1 gene that distinguishes the A/J and C57BL/6J parental strains and used to map Ephx1 to Chromosome (Chr) 1 at approximately 98.5cM (LOD = 10.0).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0938-8990
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
915-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11003708-Alleles, pubmed-meshheading:11003708-Amino Acid Sequence, pubmed-meshheading:11003708-Amino Acid Substitution, pubmed-meshheading:11003708-Animals, pubmed-meshheading:11003708-Arginine, pubmed-meshheading:11003708-Base Sequence, pubmed-meshheading:11003708-Chromosome Mapping, pubmed-meshheading:11003708-Cysteine, pubmed-meshheading:11003708-DNA, Complementary, pubmed-meshheading:11003708-Epoxide Hydrolases, pubmed-meshheading:11003708-Female, pubmed-meshheading:11003708-Genome, pubmed-meshheading:11003708-Hot Temperature, pubmed-meshheading:11003708-Mice, pubmed-meshheading:11003708-Mice, Inbred C57BL, pubmed-meshheading:11003708-Molecular Sequence Data, pubmed-meshheading:11003708-Polymorphism, Genetic, pubmed-meshheading:11003708-Sequence Homology, Amino Acid, pubmed-meshheading:11003708-Thermosensing
pubmed:year
2000
pubmed:articleTitle
The Ephx1(d) allele encoding an Arg338Cys substitution is associated with heat lability.
pubmed:affiliation
Oral Facial Genetics Program, Department of Oral Facial Development, Indiana University School of Dentistry, 1121 W. Michigan Street, DS270, Indianapolis, Indiana 46202, USA. jhartsfi@iupui.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.