G9270
γ-Glutamyltranspeptidase from equine kidney
Type VI, 5-12 units/mg solid
Synonym(s):
γ-GT, γ-Glutamyltransferase, (5-Glutamyl)peptide:amino-acid 5-glutamyltransferase, GGTP
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About This Item
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biological source
equine kidney
type
Type VI
form
solid
specific activity
5-12 units/mg solid
storage temp.
−20°C
General description
Gamma-Glutamyltranspeptidase is a heterodimeric enzyme and belongs to the superfamily of N-terminal nucleophile hydrolases.
Application
Gamma-glutamyltranspeptidase from equine kidney has been used:
- to identify the formation of 4-S-Cysteinyltetrodotoxin in the liver of Fugu pardalis
- as a standard to determine the activity of gamma-glutamyltransferase from human B-cell lymphoma cell lysates
- to hydrolyze isopeptides to study its effects on tubulin aggregation
Biochem/physiol Actions
Gamma-Glutamyltranspeptidase participates in glutathione metabolism and it catalyzes the cleavage of gamma-glutamyl compounds, such as glutathione. It also plays a role in the transfer of gamma-glutamyl moiety to amino acids and peptides.
Quality
Crude
Unit Definition
One unit will liberate 1.0 μmole of p-nitroaniline from L-γ-glutamyl-p-nitroanilide per min at pH 8.5 at 25°C.
inhibitor
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Journal of cancer research and clinical oncology, 133(12), 957-967 (2007-06-15)
The aim of this study was to characterize three new, recently established non-Hodgkin lymphoma cell lines (GUMBUS, DOGUM, and DOGKIT), isolated from patients developing high-clinical resistance to cytotoxic therapy, with respect to sensitivity toward 21 antitumor drugs from different classes
Gina Boanca et al.
The Journal of biological chemistry, 281(28), 19029-19037 (2006-05-05)
Gamma-glutamyltranspeptidase (gammaGT), a member of the N-terminal nucleophile hydrolase superfamily, initiates extracellular glutathione reclamation by cleaving the gamma-glutamyl amide bond of the tripeptide. This protein is translated as an inactive proenzyme that undergoes autoprocessing to become an active enzyme. The
Lawrence M Schopfer et al.
The Journal of biological chemistry, 293(35), 13566-13577 (2018-07-15)
Exposure to organophosphorus toxicants (OP) can have chronic adverse effects that are not explained by inhibition of acetylcholinesterase, the cause of acute OP toxicity. We therefore hypothesized that OP-induced chronic illness is initiated by the formation of organophosphorus adducts on
Mari Yotsu-Yamashita et al.
Chemical research in toxicology, 18(5), 865-871 (2005-05-17)
The metabolic pathway of tetrodotoxin (TTX), a powerful and specific voltage-gated sodium channel blocker, has not been well-clarified either in TTX-poisoned patients or in puffer fish. 4-S-CysteinylTTX (4-CysTTX) was isolated from the liver of the puffer fish, Fugu pardalis, as
H Suzuki et al.
Amino acids, 32(3), 333-340 (2006-10-13)
Some amino acids and peptides, which have low solubility in water, become much more soluble following gamma-glutamylation. Compounds become more stable in the blood stream with gamma-glutamylation. Several gamma-glutamyl compounds are known to have favorable physiological effects on mammals. Gamma-glutamylation
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