Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin.
CM Lee, SH Snyder - Journal of Biological Chemistry, 1982 - Elsevier
CM Lee, SH Snyder
Journal of Biological Chemistry, 1982•ElsevierThe cytosolic dipeptidyl-aminopeptidase III (EC 3.4. 14.4) from rat brain was partially purified
using Arg-Arg-4-methoxy-beta-naphthylamide as a substrate. It was completely separated
from aminopeptidase B on DEAE-Sephacel ion exchange chromatography. Similar to
bovine pituitary dipeptidyl-aminopeptidase III, it has a pH optimum of 9, prefers Arg-Arg-4-
methoxy-beta-naphthylamide as a substrate, and catalyzes the sequential release of
dipeptides from the NH2 terminus of peptide substrates provided they are not smaller than a …
using Arg-Arg-4-methoxy-beta-naphthylamide as a substrate. It was completely separated
from aminopeptidase B on DEAE-Sephacel ion exchange chromatography. Similar to
bovine pituitary dipeptidyl-aminopeptidase III, it has a pH optimum of 9, prefers Arg-Arg-4-
methoxy-beta-naphthylamide as a substrate, and catalyzes the sequential release of
dipeptides from the NH2 terminus of peptide substrates provided they are not smaller than a …
The cytosolic dipeptidyl-aminopeptidase III (EC 3.4.14.4) from rat brain was partially purified using Arg-Arg-4-methoxy-beta-naphthylamide as a substrate. It was completely separated from aminopeptidase B on DEAE-Sephacel ion exchange chromatography. Similar to bovine pituitary dipeptidyl-aminopeptidase III, it has a pH optimum of 9, prefers Arg-Arg-4-methoxy-beta-naphthylamide as a substrate, and catalyzes the sequential release of dipeptides from the NH2 terminus of peptide substrates provided they are not smaller than a tetrapeptide. Among numerous biologically active peptides tested, angiotensins and enkephalins were the most preferred substrates with micromolar affinities, suggesting that dipeptidyl-aminopeptidase III may play a physiologic role in regulating enkephalin and/or angiotensin disposition.
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