|  Help  |  About  |  Contact Us

Publication : Subunit Va of human and bovine cytochrome c oxidase is highly conserved.

First Author  Rizzuto R Year  1988
Journal  Gene Volume  69
Issue  2 Pages  245-56
PubMed ID  2853101 Mgi Jnum  J:9661
Mgi Id  MGI:58118 Doi  10.1016/0378-1119(88)90435-0
Citation  Rizzuto R, et al. (1988) Subunit Va of human and bovine cytochrome c oxidase is highly conserved. Gene 69(2):245-56
abstractText  We have isolated a full-length cDNA clone specifying the nuclear-encoded subunit Va of the human mitochondrial respiratory enzyme cytochrome c oxidase (COX; EC 1.9.3.1.). The deduced sequence of the polypeptide is 95% identical to that of the corresponding subunit of bovine COX, which makes it the most conserved polypeptide among the known bovine/human pairs of COX subunits. This polypeptide contains an N-terminal presequence which is rich in basic and hydroxylated residues, but differs from the deduced presequences of all other previously isolated COX subunits in that it also contains a negatively charged residue. We find no evidence of tissue-specific isoforms of subunit Va, as Northern analysis showed a single, identically-sized transcript in RNA from human muscle, liver, and brain, while coxVa cDNAs isolated from both endothelial and fetal muscle cDNA libraries had identical nucleotide sequences.
Quick Links:
 
Quick Links:
 

Expression

Publication --> Expression annotations

 

Other

1 Bio Entities

Trail: Publication

0 Expression