L-Glutamine 7-amido-4-methylcoumarin
Need Assistance?
  • US & Canada:
    +
  • UK: +

L-Glutamine 7-amido-4-methylcoumarin

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category
L-Amino Acids
Catalog number
BAT-005864
CAS number
105888-45-7
Molecular Formula
C15H17N3O4
Molecular Weight
303.31
L-Glutamine 7-amido-4-methylcoumarin
IUPAC Name
(2S)-2-amino-N-(4-methyl-2-oxochromen-7-yl)pentanediamide
Synonyms
H-Gln-AMC
Purity
95%
InChI
InChI=1S/C15H17N3O4/c1-8-6-14(20)22-12-7-9(2-3-10(8)12)18-15(21)11(16)4-5-13(17)19/h2-3,6-7,11H,4-5,16H2,1H3,(H2,17,19)(H,18,21)/t11-/m0/s1
InChI Key
VEPDWBJBPXVCEN-NSHDSACASA-N
Canonical SMILES
CC1=CC(=O)OC2=C1C=CC(=C2)NC(=O)C(CCC(=O)N)N
1. Changes in the kinetic parameters of hepatic gamma-glutamyltransferase from streptozotocin-induced diabetic rats
P D Cornwell, J B Watkins 3rd Biochim Biophys Acta. 2001 Feb 9;1545(1-2):184-91. doi: 10.1016/s0167-4838(00)00276-4.
Previous research has shown that the enzymatic activity of hepatic gamma-glutamyltransferase was increased in streptozotocin-induced diabetic rats with no increase in the expression of the protein. The current work has characterized the differences in the kinetic properties of hepatic gamma-glutamyltransferase from diabetic versus control rats. Hepatic gamma-glutamyltransferase was purified from control male and female rats and from rats made diabetic 30 days previously with streptozotocin. The maximal velocity and the Michaelis constant were determined for the purified enzyme with two separate donors (L-gamma-glutamyl-p-nitroanilide or L-gamma-glutamyl-(7-amido-4-methylcoumarin)) in the presence of one of eight acceptors (L-alanine-glycine, L-glycine-glycine, L-methionine, L-glutamate, L-alanine, L-glutamine, L-phenylalanine or L-aspartate). With both donors, hepatic gamma-glutamyltransferase from diabetic rats had a consistently higher kinetic efficiency than gamma-glutamyltransferase from controls. The kinetic efficiency percent increase of diabetic over control gamma-glutamyltransferase when averaged across all acceptors was higher in males than in females. With L-gamma-glutamyl-p-nitroanilide, the kinetic efficiency increase of diabetic over control gamma-glutamyltransferase was higher with poor acceptors than with highly efficient acceptors. These data indicate that there are differences in the physical properties of hepatic gamma-glutamyltransferase from diabetic versus control rats and from female versus male rats.
2. Electrophoretic studies of serum gamma-glutamyl transferase from patients with hepatoma
K D Hammond, M J Gravenor, D Piesas Ann Clin Biochem. 1985 Jul;22 ( Pt 4):376-80. doi: 10.1177/000456328502200408.
Activities and isoenzyme patterns of gamma-glutamyl transferase (GGT) were studied in serum samples from fifteen Bantu males suffering from primary hepatoma; the results were compared with those obtained from normal samples. Enzyme activities were significantly higher in hepatoma patients than in controls. Results with Cellogel electrophoresis and the fluorescent substrate gamma-L-glutamine-7-amido-4-methylcoumarin were reproducible; two major bands of activity were observed in normal serum and three bands in hepatoma serum. The additional band seen in hepatoma serum was also detected in serum from patients with certain other disorders. With polyacrylamide gel electrophoresis using either gamma-L-glutamyl-alpha-naphthylamide or gamma-L-glutamyl-p-nitroanilide as substrates, results were inconsistent and difficult to interpret since there was a lack of specificity for GGT.
Online Inquiry
Verification code
Inquiry Basket