A1271
Adenosine 5′-monophosphate–Agarose
lyophilized powder
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About This Item
MDL number:
UNSPSC Code:
41106500
eCl@ss:
32160414
PubChem Substance ID:
NACRES:
NA.56
Recommended Products
biological source
plant (Sea weed)
Quality Level
form
lyophilized powder
extent of labeling
1-5 μmol per mL
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
C-8
matrix spacer
9 atoms
storage temp.
−20°C
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Application
Adenosine 5′-monophosphate Agarose (5′-AMP agarose) has been used in affinity chromatography to isolate β and gamma glutamate decarboxylase, which is important for controlling gamma-aminobutyric acid (GABA) synthesis in brain.
Physical form
Lyophilized powder stabilized with lactose
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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S M Pettit et al.
Clinical chemistry, 27(1), 88-93 (1981-01-01)
We present a method for preparing human liver lactate dehydrogenase (L-lactate:NAD+ oxidoreductase; EC 1.1.1.27) isoenzyme-5 by sequential ion-exchange chromatography, general-ligand (AMP analog) affinity chromatography, and preparative isoelectric focusing. The yield ws 40%, with a 493-fold purification. The final specific activity
D W Parkin
The Journal of biological chemistry, 271(36), 21713-21719 (1996-09-06)
Trypanosomes have no de novo purine biosynthesis and thus depend upon salvage pathways to obtain purines for their metabolic pathways and for the biosynthesis of nucleic acids. An inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-nucleoside hydrolase) from the African trypanosome Trypanosoma brucei
D M Brown et al.
European journal of biochemistry, 241(1), 155-161 (1996-10-01)
We describe the purification of a H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. The enzyme is a monomeric flavoprotein containing flavin adenine dinucleotide in a 1:1 molar ratio with the polypeptide. The NADH oxidase has an apparent molecular
S J Wu et al.
Journal of neurochemistry, 42(6), 1607-1612 (1984-06-01)
The interactions of two forms of porcine brain glutamate decarboxylase (beta-GAD and gamma-GAD) with the effector ATP were studied by affinity chromatography. A third form, alpha-GAD, was only slightly retarded by the affinity matrix and was eluted in the buffer
D L Martin et al.
Journal of neurochemistry, 55(2), 524-532 (1990-08-01)
A major regulatory feature of brain glutamate decarboxylase (GAD) is a cyclic reaction that controls the relative amounts of holoenzyme and apoenzyme [active and inactive GAD with and without bound pyridoxal 5'-phosphate (pyridoxal-P, the cofactor), respectively]. Previous studies have indicated
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