Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4+ and CD8+ spleen T cells

B. C. Miller; Dwain L Thiele; L. B. Hersh; G. L. Cottam

doi:10.1006/abbi.1994.1223

Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4⁺ and CD8⁺ spleen T cells

B. C. Miller, Dwain L Thiele, L. B. Hersh, G. L. Cottam

Internal Medicine

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Exogenous methionine enkephalin incubated with CD4⁺ or CD8⁺ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC 3.4.11.2), a membrane-anchored ectopeptidase. The enzyme activity is identified by its substrate specificity, sensitivity to inhibition by amastatin, and immunoreactivity with antibody to rat kidney aminopeptidase N. Activation of CD4⁺ T cells results in a small increase per cell in aminopeptidase N activity.

Original language	English (US)
Pages (from-to)	174-179
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	311
Issue number	1
DOIs	https://doi.org/10.1006/abbi.1994.1223
State	Published - May 1994

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4+ and CD8+ spleen T cells",

abstract = "Exogenous methionine enkephalin incubated with CD4+ or CD8+ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC 3.4.11.2), a membrane-anchored ectopeptidase. The enzyme activity is identified by its substrate specificity, sensitivity to inhibition by amastatin, and immunoreactivity with antibody to rat kidney aminopeptidase N. Activation of CD4+ T cells results in a small increase per cell in aminopeptidase N activity.",

author = "Miller, {B. C.} and Thiele, {Dwain L} and Hersh, {L. B.} and Cottam, {G. L.}",

year = "1994",

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AU - Cottam, G. L.

PY - 1994/5

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N2 - Exogenous methionine enkephalin incubated with CD4+ or CD8+ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC 3.4.11.2), a membrane-anchored ectopeptidase. The enzyme activity is identified by its substrate specificity, sensitivity to inhibition by amastatin, and immunoreactivity with antibody to rat kidney aminopeptidase N. Activation of CD4+ T cells results in a small increase per cell in aminopeptidase N activity.

AB - Exogenous methionine enkephalin incubated with CD4+ or CD8+ T cells purified from murine spleen is metabolized primarily, if not exclusively, by aminopeptidase N (aminopeptidase M, EC 3.4.11.2), a membrane-anchored ectopeptidase. The enzyme activity is identified by its substrate specificity, sensitivity to inhibition by amastatin, and immunoreactivity with antibody to rat kidney aminopeptidase N. Activation of CD4+ T cells results in a small increase per cell in aminopeptidase N activity.

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Methionine enkephalin is hydrolyzed by aminopeptidase N on CD4⁺ and CD8⁺ spleen T cells

Abstract

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