Mouse carbonic anhydrase III: Nucleotide sequence and expression studies
- 1 February 1989
- journal article
- research article
- Published by Springer Nature in Biochemical Genetics
- Vol. 27 (1-2) , 17-30
- https://doi.org/10.1007/bf00563015
Abstract
A cDNA for the mouse carbonic anhydrase, CAIII, has been isolated from a λgt11 expression library. The cloned cDNA contains all of the coding region (777 bp) and both 5′ untranslated (86-bp) and 3′ untranslated (217-bp) sequences. The coding sequence shows 87% homology at the nucleotide level and 91% homology, when amino acid residues are compared, with human CAIII. Protein and mRNA analyses show that CAIII is present at low levels in cultured myoblasts and is abundant in adult skeletal muscle and in liver. The marked sex-related differences in CAIII distribution, described for rat liver, are not seen in the mouse. Restriction fragment length polymorphisms usingTaqI andPstI are described which distinguish betweenMus spretus andMus musculus domesticus.Keywords
This publication has 41 references indexed in Scilit:
- Detection of specific sequences among DNA fragments separated by gel electrophoresisPublished by Elsevier ,2006
- Molecular evolution of the carbonic anhydrase genes: Calculation of divergence time for mouse carbonic anhydrase I and IIJournal of Molecular Evolution, 1986
- Assignment of the gene determining human carbonic anhydrase, CAI, to chromosome 8Annals of Human Genetics, 1986
- The gene for human muscle specific carbonic anhydrase (CA III) is assigned to chromosome 8Annals of Human Genetics, 1986
- Isolation of a cDNA clone for the human muscle specific carbonic anhydrase, CAIIIAnnals of Human Genetics, 1985
- Testosterone-induced, sulfonamide-resistant carbonic anhydrase isozyme of rat liver is indistinguishable from skeletal muscle carbonic anhydrase IIIFEBS Letters, 1981
- Specific changes in cellular glycoproteins and surface proteins during myogenesis in clonal muscle cellsDevelopmental Biology, 1981
- At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptideJournal of Molecular Biology, 1978
- Basic muscle protein, a third genetic locus isoenzyme of carbonic anhydrase?Biochemical and Biophysical Research Communications, 1977
- Evolution of mammalian carbonic anhydrase loci by tandem duplication: Close linkage of Car-1 and Car-2 to the centromere region of chromosome 3 of the mouseBiochemical Genetics, 1976