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
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
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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
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 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
Cellular and molecular neurobiology, 7(3), 237-253 (1987-09-01)
1. Glutamate decarboxylase is a focal point for controlling gamma-aminobutyric acid (GABA) synthesis in brain. Several factors that appear to be important in the regulation of GABA synthesis have been identified by relating studies of purified glutamate decarboxylase to conditions
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