Measurement of glutamate carboxypeptidase II (NAALADase) enzyme activity by the hydrolysis of [ 3H]-N-acetylaspartylglutamate (NAAG).

Carol W Tiffany, Barbara Slusher

Research output: Contribution to journalArticle

Abstract

The peptide N-Acetylaspartylglutamate (NAAG) is hydrolyzed by N-Acetylated-alpha-linked-acidic dipeptidase (NAALADase, glutamate carboxypeptidase II) into N-Acetylated aspartate (NAA) and glutamate. Hydrolysis can be measured as described in this unit by employing radiolabeled NAAG (NAA-[(3)H]glu) as the substrate. The occurrence of NAALADase activity in a wide range of tissues has implications for a variety of physiological purposes. The assay described here is useful for the analysis of NAALADase activity and its inhibition in brain synaptosomal preparations, tissue homogenates and tissue culture cell pellets.

Original languageEnglish (US)
JournalCurrent protocols in pharmacology / editorial board, S.J. Enna (editor-in-chief) ... [et al.]
VolumeChapter 3
StatePublished - Feb 2002
Externally publishedYes

Fingerprint

Glutamate Carboxypeptidase II
Hydrolysis
Enzymes
Aspartic Acid
Glutamic Acid
Cell Culture Techniques
N-acetyl-1-aspartylglutamic acid
Peptides
Brain

ASJC Scopus subject areas

  • Medicine(all)

Cite this

@article{ac3fe1e4de9b491aa53f3ad360107ced,
title = "Measurement of glutamate carboxypeptidase II (NAALADase) enzyme activity by the hydrolysis of [ 3H]-N-acetylaspartylglutamate (NAAG).",
abstract = "The peptide N-Acetylaspartylglutamate (NAAG) is hydrolyzed by N-Acetylated-alpha-linked-acidic dipeptidase (NAALADase, glutamate carboxypeptidase II) into N-Acetylated aspartate (NAA) and glutamate. Hydrolysis can be measured as described in this unit by employing radiolabeled NAAG (NAA-[(3)H]glu) as the substrate. The occurrence of NAALADase activity in a wide range of tissues has implications for a variety of physiological purposes. The assay described here is useful for the analysis of NAALADase activity and its inhibition in brain synaptosomal preparations, tissue homogenates and tissue culture cell pellets.",
author = "Tiffany, {Carol W} and Barbara Slusher",
year = "2002",
month = "2",
language = "English (US)",
volume = "Chapter 3",
journal = "Current Protocols in Pharmacology",
issn = "1934-8282",
publisher = "John Wiley and Sons Inc.",

}

TY - JOUR

T1 - Measurement of glutamate carboxypeptidase II (NAALADase) enzyme activity by the hydrolysis of [ 3H]-N-acetylaspartylglutamate (NAAG).

AU - Tiffany, Carol W

AU - Slusher, Barbara

PY - 2002/2

Y1 - 2002/2

N2 - The peptide N-Acetylaspartylglutamate (NAAG) is hydrolyzed by N-Acetylated-alpha-linked-acidic dipeptidase (NAALADase, glutamate carboxypeptidase II) into N-Acetylated aspartate (NAA) and glutamate. Hydrolysis can be measured as described in this unit by employing radiolabeled NAAG (NAA-[(3)H]glu) as the substrate. The occurrence of NAALADase activity in a wide range of tissues has implications for a variety of physiological purposes. The assay described here is useful for the analysis of NAALADase activity and its inhibition in brain synaptosomal preparations, tissue homogenates and tissue culture cell pellets.

AB - The peptide N-Acetylaspartylglutamate (NAAG) is hydrolyzed by N-Acetylated-alpha-linked-acidic dipeptidase (NAALADase, glutamate carboxypeptidase II) into N-Acetylated aspartate (NAA) and glutamate. Hydrolysis can be measured as described in this unit by employing radiolabeled NAAG (NAA-[(3)H]glu) as the substrate. The occurrence of NAALADase activity in a wide range of tissues has implications for a variety of physiological purposes. The assay described here is useful for the analysis of NAALADase activity and its inhibition in brain synaptosomal preparations, tissue homogenates and tissue culture cell pellets.

UR - http://www.scopus.com/inward/record.url?scp=84857392621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84857392621&partnerID=8YFLogxK

M3 - Article

VL - Chapter 3

JO - Current Protocols in Pharmacology

JF - Current Protocols in Pharmacology

SN - 1934-8282

ER -