Characterization of Membrane‐Bound Aminopeptidases from Rat Brain: Identification of the Enkephalin‐Degrading Aminopeptidase

Characterization of Membrane‐Bound Aminopeptidases from Rat Brain: Identification of the... Abstract: Rat brain aminopeptidase activity was solubilized from membranes by incubation with thiols. This novel procedure resulted in the release of the same two aminopeptidases (MI and MII) previously shown to be solubilized by the nonionic detergent Triton X‐100. The solubilized aminopeptidases MI and MII were resolved by ion‐exchange chromatography and further purified by hydroxylapatite chromatography. Aminopeptidase MI was shown to hydrolyze only the β‐naphthylamides of arginine and lysine whereas aminopeptidase MII exhibited a broad specificity with respect to amino acid β‐naphthylamides. Only aminopeptidase MII hydrolyzed Leu‐enkephalin at a significant rate, indicating that this enzyme can account for the membrane‐bound enkephalin aminopeptidase activity. The enkephalin‐degrading aminopeptidase is potently inhibited by opioid (α‐neo‐endorphin and dynorphin) as well as nonopioid (substance P, somatostatin, and angiotensin I) peptides in the range of 0.2–2.0 μM The regional distribution of aminopeptidases MI and MII in rat brain are rather different, with aminopeptidase MII distribution more closely paralleling the distribution of opiate receptors. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

Characterization of Membrane‐Bound Aminopeptidases from Rat Brain: Identification of the Enkephalin‐Degrading Aminopeptidase

Journal of Neurochemistry, Volume 44 (5) – May 1, 1985

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Publisher
Wiley
Copyright
Copyright © 1985 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
DOI
10.1111/j.1471-4159.1985.tb08779.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: Rat brain aminopeptidase activity was solubilized from membranes by incubation with thiols. This novel procedure resulted in the release of the same two aminopeptidases (MI and MII) previously shown to be solubilized by the nonionic detergent Triton X‐100. The solubilized aminopeptidases MI and MII were resolved by ion‐exchange chromatography and further purified by hydroxylapatite chromatography. Aminopeptidase MI was shown to hydrolyze only the β‐naphthylamides of arginine and lysine whereas aminopeptidase MII exhibited a broad specificity with respect to amino acid β‐naphthylamides. Only aminopeptidase MII hydrolyzed Leu‐enkephalin at a significant rate, indicating that this enzyme can account for the membrane‐bound enkephalin aminopeptidase activity. The enkephalin‐degrading aminopeptidase is potently inhibited by opioid (α‐neo‐endorphin and dynorphin) as well as nonopioid (substance P, somatostatin, and angiotensin I) peptides in the range of 0.2–2.0 μM The regional distribution of aminopeptidases MI and MII in rat brain are rather different, with aminopeptidase MII distribution more closely paralleling the distribution of opiate receptors.

Journal

Journal of NeurochemistryWiley

Published: May 1, 1985

References

  • An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin
    Hersh, Hersh; McKelvy, McKelvy
  • Enkephalin dipeptidyl carboxypeptidase (enkephalinase) activity: selective radioassay, properties, and regional distribution in human brain
    Llorens, Llorens; Malfroy, Malfroy; Schwartz, Schwartz; Gacel, Gacel; Roques, Roques; Roy, Roy; Morgat, Morgat; Javoy‐Agid, Javoy‐Agid; Agid, Agid

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