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Key Documents

G1642

Sigma-Aldrich

sn-Glycerol-3-phosphocholine Phosphodiesterase from mold

lyophilized powder, ≥5 units/mg protein

Synonym(s):

Glycerophosphorylcholine phosphodiesterase from mold

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥5 units/mg protein

composition

Protein, ~40% Bradford

storage temp.

−20°C

Unit Definition

One unit will produce 1.0 μmole of choline from L-α-glycerophosphorylcholine, G4007, per min at pH 8.0 at 37 °C.

Physical form

Lyophilized powder containing Tris buffer salt

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)

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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Mária Simocková et al.
The Journal of biological chemistry, 283(25), 17107-17115 (2008-04-25)
The product of the open reading frame YPL206c, Pgc1p, of the yeast Saccharomyces cerevisiae displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases. Deletion of PGC1 causes an accumulation of the anionic phospholipid, phosphatidylglycerol (PG), especially under conditions of inositol limitation.
Carmelina D Anfuso et al.
Lipids, 38(1), 45-52 (2003-04-03)
In pericytes from bovine retina, the enzyme glycerophosphocholine phosphodiesterase, catalyzing the hydrolysis of sn-glycero-3-phosphocholine to glycero-3-phosphate and choline, has been characterized with respect to pH optimum, metal ion dependence, Km, inhibitors, and subcellular localization. In these cells, the natural substrate
J P Galons et al.
Magnetic resonance in medicine, 33(3), 422-426 (1995-03-01)
The purpose of this study was to study the metabolic events during a slow acidosis in three different cell lines by combining 31P magnetic resonance spectroscopy and hollow fiber bioreactor technology. The rate of change in intracellular pH, glycerophosphorylcholine (GPC)
C D Anfuso et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 112(3), 493-501 (1995-11-01)
While steady-state kinetic parameters (metabolite pools, Km and activation energies) are partially known for the enzymes involved in phosphatidylcholine synthesis and degradation in mammalian brain, they are not available for the nervous system of lower vertebrates or invertebrates. Since the
S Sipione et al.
FEBS letters, 384(1), 19-24 (1996-04-08)
In microvessels isolated from bovine brain, microsomal enzyme activities involved in phosphatidylcholine biosynthesis and degradation were determined. The microvessels possessed acyl-CoA:1-acyl-sn-glycero-3-phosphocholine (AT) and glycerophosphocholine phosphodiesterase (GroPChoPDE) activity at a higher level compared with bovine and rat brain or rat liver

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