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 se...

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Bibliographic Details
Published in:The Journal of biological chemistry 1989-10, Vol.264 (28), p.16754-16758
Main Authors: KUMAR, R. S, KUSARI, J, ROY, S. N, SOFFER, R. L, SEN, G. C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Base Sequence
Biological and medical sciences
Cloning, Molecular
DNA - genetics
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
genes
Hydrolases
Isoenzymes - genetics
Lung - enzymology
Male
Molecular Sequence Data
Mosaicism
Peptidyl-Dipeptidase A - genetics
Protein Conformation
Rabbits
Sequence Homology, Nucleic Acid
testes
Testis - enzymology
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Summary: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.
ISSN:0021-9258
1083-351X