G1642
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:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥5 units/mg protein
form
lyophilized powder
specific activity
≥5 units/mg protein
composition
Protein, ~40% Bradford
storage temp.
−20°C
Quality Level
Physical form
Lyophilized powder containing Tris buffer salt
Other Notes
One unit will produce 1.0 μmole of choline from L-α-glycerophosphorylcholine, G4007, per min at pH 8.0 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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J N Kanfer et al.
Neurochemical research, 18(3), 331-334 (1993-03-01)
Previous studies have demonstrated elevated brain levels of phosphomonoesters in early stages of Alzheimer's disease and elevations of phosphodiesters later in the disease. In addition, preliminary quantitative analyses of the phospholipids of Alzheimer's brain reveals either decreases in some phospholipids
J Yuan et al.
Neurochemical research, 19(1), 43-48 (1994-01-01)
An enzyme releasing phosphocholine from glycerophosphocholine was purified to apparent homogeneity based upon SDS-PAGE. The enzyme was liberated from lyophilized bovine myelin by differential detergent extraction and final purification was accomplished with Q-Sepharose Fast Flow chromatography yielding an apparently homogeneous
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
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
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