Abstract:
:A full-length cDNA for dopamine beta-monooxygenase (D beta M) from bovine adrenal glands has been cloned and sequenced. The soluble and membrane-derived forms of D beta M have also been sequenced from their N-termini. While the observed sequences for the soluble protein correspond to those previously reported [Joh, T.H., & Hwang, O. (1986) Ann. N.Y. Acad. Sci. 493, 343-350], the heavy subunit of membrane-derived enzyme is found to contain a unique N-terminus. Alignment of this N-terminus with that deduced from cDNA cloning indicates identity at 22 (and possibly 26) out of 27 residues. This comparison leads us to conclude that the membranous form of bovine D beta M retains an uncleaved N-terminal signal peptide as the source of membrane anchoring.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Taljanidisz J,Stewart L,Smith AJ,Klinman JPdoi
10.1021/bi00452a026subject
Has Abstractpub_date
1989-12-26 00:00:00pages
10054-61issue
26eissn
0006-2960issn
1520-4995journal_volume
28pub_type
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