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(Received for publication, July 29, 1996, and in revised form, September 3, 1996)
From the Department of Molecular Pharmacology, Albert Einstein
College of Medicine, Bronx, New York 10461
Metallocarboxypeptidase D (CPD) is a recently
discovered 180-kDa membrane-bound carboxypeptidase E-like enzyme (Song,
L. and Fricker, L. D. (1995) J. Biol. Chem. 270, 25007-25013). In the present study, a soluble CPD-like activity has
been purified to homogeneity and characterized. On denaturing
polyacrylamide gels, the soluble enzyme from bovine pituitary glands
appears as two bands of 170 and 135 kDa which are converted to 155 and
115 kDa by endoglycosidase F. Both of the soluble forms of CPD are
recognized by an antisera raised against CPD purified from rat brain
membranes. The partial N-terminal amino acid sequences of the two
soluble forms are identical to each other and to the predicted N
terminus of duck gp180. The soluble and membrane forms of CPD have
similar pH optima, inhibitor specificities, and kinetic parameters for substrate hydrolysis. CPD-like enzymatic activity is detected in all
rat tissues examined, with highest levels in pituitary, brain, and
adrenal. Western blot analysis indicates that both soluble and membrane
forms of CPD are present in rat brain, heart, liver, and kidney. At
least four distinct 100-180-kDa forms of CPD are detected on Western
blots, although an antiserum raised against the C-terminal region of
rat CPD recognizes only the 180-kDa membrane-bound form. The finding
that CPD is widely distributed suggests a broad role for this enzyme in
the processing of proteins that transit the secretory pathway.
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28884-28889
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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