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Peptide hormones are synthesized from larger precursors by cleavages at paired basic residues. We have isolated a pro-hormone converting enzyme from bovine neural and intermediate lobe secretory vesicles that cleaves pro-vasopressin and pro-opiomelanocortin at Lys-Arg residues to yield vasopressin, and adrenocorticotropin/endorphin-related peptides, respectively. The enzyme from both lobes is an aspartyl protease of approximately 70,000 Da, is a glycoprotein and has an optimum pH range of 4.0-5.0. Present within the same secretory vesicles is an aminopeptidase B-like enzyme which is a metalloprotease that is inhibited by Co2+ and Zn2+. This enzyme may play a role in trimming off the N-terminal extended basic residues from peptides liberated by the pro-hormone converting enzyme.
Y P Loh, and
N P Birch, and
M G Castro
June 1985,
The Journal of biological chemistry,
Y P Loh, and
N P Birch, and
M G Castro
September 1986,
The Journal of biological chemistry,
Y P Loh, and
N P Birch, and
M G Castro
January 1995,
Methods in enzymology,
Y P Loh, and
N P Birch, and
M G Castro
May 1985,
FEBS letters,
Y P Loh, and
N P Birch, and
M G Castro
September 1988,
FEBS letters,
Y P Loh, and
N P Birch, and
M G Castro
April 1983,
Regulatory peptides,
Y P Loh, and
N P Birch, and
M G Castro
November 1986,
The Journal of biological chemistry,
Y P Loh, and
N P Birch, and
M G Castro
May 1984,
Proceedings of the National Academy of Sciences of the United States of America,
Y P Loh, and
N P Birch, and
M G Castro
August 1983,
FEBS letters,
Y P Loh, and
N P Birch, and
M G Castro
January 1982,
Proceedings of the National Academy of Sciences of the United States of America,
