Bovine lung angiotensin-converting enzyme was isolated in pure form and the sequence of the first twenty-two NH2-terminal amino acids determined. Oligonucleotides, complementary to a selected portion of the NH2-terminal amino acid sequence of the bovine glycoprotein (Mr 145,000), were synthesized and used for hybridization selection of angiotensin-converting enzyme mRNA. The hybridization-selected mRNA programmed the in vitro synthesis of a single polypeptide (Mr 130,000) that was specifically immunoadsorbed by anti- bovine enzyme antibodies. Preliminary sequence analysis of the primary translation product suggests that bovine angiotensin-converting enzyme is synthesized without a transient NH2-terminal signal sequence.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 30 1986|
Bibliographical noteFunding Information:
This investigation was supported by National Institutes of Health Grant AM 19850. DCS is recipient of an NHLBI Clinical Investigator Award HL01176. The authors dedicate this paper to Dr. Edward C. Heath who created the critical scientific environment for this study but whose untimely death preceded the preparation of this manuscript.
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology