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A1271

Sigma-Aldrich

Adenosine 5′-monophosphate–Agarose

lyophilized powder

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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

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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 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
F James et al.
The Journal of biological chemistry, 270(38), 22344-22350 (1995-09-22)
The plant enzyme S-adenosylmethionine:methionine S-methyltransferase (EC 2.1.1.12, MMT) catalyzes the synthesis of S-methylmethionine. MMT was purified 620-fold to apparent homogeneity from leaves of Wollastonia biflora. The four-step purification included fractionation with polyethylene glycol, affinity chromatography on adenosine-agarose, anion exchange chromatography

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