THE DEDUCED AMINO-ACID-SEQUENCE OF HUMAN CARBONIC ANHYDRASE-RELATED PROTEIN (CARP) IS 98-PERCENT IDENTICAL TO THE MOUSE HOMOLOG

Citation
La. Skaggs et al., THE DEDUCED AMINO-ACID-SEQUENCE OF HUMAN CARBONIC ANHYDRASE-RELATED PROTEIN (CARP) IS 98-PERCENT IDENTICAL TO THE MOUSE HOMOLOG, Gene, 126(2), 1993, pp. 291-292
Citations number
7
Categorie Soggetti
Genetics & Heredity
Journal title
GeneACNP
ISSN journal
03781119
Volume
126
Issue
2
Year of publication
1993
Pages
291 - 292
Database
ISI
SICI code
0378-1119(1993)126:2<291:TDAOHC>2.0.ZU;2-9
Abstract
A recently reported mRNA, encoding 'carbonic anhydrase-related polypep tide' (CARP) from the Purkinje cells of mouse cerebellum, was shown to have a 30-40% deduced amino acid sequence identity with the carbonic anhydrases (CA) of mammals. In order to compare the mouse and human CA RP sequences, we used the polymerase chain reaction (PCR) to amplify h uman CARP sequences from several cDNA libraries (salivary gland, testi s and placenta). The sequence has an 89.3% sequence identity with mous e CARP at the nucleotide level and 97.9% at the amino acid level. This extremely high evolutionary conservation suggests an important functi on for the CARP gene product.