Bovine angiotensin-converting enzyme: amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002474:Cell-Free System; D007163:Immunosorbent Techniques; D008168:Lung / Q000032:analysis; D009693:Nucleic Acid Hybridization; D009838:Oligodeoxyribonucleotides / Q000235:genetics; D010446:Peptide Fragments; D007703:Peptidyl-Dipeptidase A / Q000235:genetics*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics
D009838:Oligodeoxyribonucleotides; D010446:Peptide Fragments; D012333:RNA, Messenger; D007703:Peptidyl-Dipeptidase A