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- Title
Triosephosphate isomerase activity-deficient mice show haemolytic anaemia in homozygous condition.
- Abstract
SummaryA triosephosphate isomerase (TPI) mutant, Tpi1a-m6Neu, with approximately 57% residual enzyme activity in blood compared with wild-type was detected among offspring of triethylenemelamine-treated male mice. Homozygous mutants with about 13% residual enzyme activity were recovered in progeny of inter sematings of heterozygotes. The loss of TPI activity was evident both in blood and in other tissue extracts. Values for haematocrit, haemoglobin, number of red blood cells (RBC), mean corpuscular volume of RBC, mean corpuscular haemoglobin concentration and spleen weight show significant differences between wild-type animals and homozygous mutants. Sequence analysis revealed a substitution (c.A149G) in the Tpi1gene. This mutation results in an Asp to Gly substitution at codon 49 in exon 2 at a highly conserved position located in the functional domain of the TPI protein which is responsible for the correct dimerization of the subunits. As a potential animal model, Tpi1a-m6Neurepresents the only available TPI-deficient homozygous viable mouse mutation.
- Subjects
TRIOSE-phosphate isomerase; ENZYME activation; HEMOLYTIC anemia; GENETIC mutation; ERYTHROCYTES; HEMOGLOBINS; LABORATORY mice; TISSUE extracts
- Publication
Genetics Research, 2009, Vol 91, Issue 1, p1
- ISSN
0016-6723
- Publication type
Article
- DOI
10.1017/S0016672308009944