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J. Biol. Chem., Vol. 265, Issue 5, 2476-2482, Feb, 1990
LD Fricker, B Das and RH Angeletti
Carboxypeptidase E (CPE), a peptide hormone-processing enzyme, is present
within secretory granules in both a soluble form and a form which is
membrane-bound at pH 5.5 but soluble at neutral pH. Antisera raised against
a peptide corresponding to the predicted COOH-terminus of CPE bind to the
membrane-associated form of CPE but not to the soluble form. This
COOH-terminal region is predicted to form an amphiphilic alpha-helix,
containing several pairs of hydrophobic residues separated by hydrophilic
residues. Synthetic COOH-terminal peptides 11-24 residues in length are
able to bind to bovine pituitary membranes and can be extracted by
conditions that extract the membrane- bound form of CPE. The influence of
pH on the membrane binding of a 21- residue COOH-terminal peptide is
similar to the membrane binding of CPE: at pH values less than 6 the
majority of the peptide is membrane- bound, while at pH values above 8 less
than 20% is membrane-bound. Both the 21-residue COOH-terminal peptide and
the purified membrane form of CPE, but not the soluble form, partition into
Triton X-114 only at low pH (pH less than 6). Combined polar and
hydrophobic interactions of the COOH-terminal peptide appear to be
responsible for the reversible, pH- dependent association of CPE with
membranes.
Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10)
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
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