Structure of testicular angiotensin-converting enzyme. A segmental mosaic isozyme.
The complete amino acid sequence of rabbit testicular angiotensin-converting enzyme has been deduced from the sequence of the corresponding cDNA clone. A protein of the expected molecular weight of 84,000 was translated in vitro from the mRNA encoded by this cDNA. All of the previously determined sequences of seven tryptic peptides from the enzyme are present in the deduced sequence, thus confirming the identity of the protein. From the deduced sequence it appears that the protein contains a signal peptide at the amino terminus and a hydrophobic anchoring domain near the carboxyl terminus. Northern analysis with oligonucleotide probes, whose sequences represented different regions of the cDNA, revealed not only the regions of extensive homology between the mRNAs encoding the testicular and the pulmonary isozymes but also a stretch of sequence near the 5' end unique to the testicular mRNA.
Kumar
R S
RS
Department of Molecular Biology, Cleveland Clinic Foundation, Ohio 44195.
Kusari
J
J
Roy
S N
SN
Soffer
R L
RL
Sen
G C
GC
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D007527:Isoenzymes / Q000235:genetics; D008168:Lung / Q000201:enzymology; D008297:Male; D008969:Molecular Sequence Data; D009030:Mosaicism; D007703:Peptidyl-Dipeptidase A / Q000235:genetics*; D011487:Protein Conformation; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D013737:Testis / Q000201:enzymology*
D007527:Isoenzymes; D004247:DNA; D007703:Peptidyl-Dipeptidase A