G1642
sn-Glycerol-3-phosphocholine Phosphodiesterase from mold
lyophilized powder, ≥5 units/mg protein
Synonym(s):
Glycerophosphorylcholine phosphodiesterase from mold
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10 UNITS
€366.00
€366.00
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10 UNITS
€366.00
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
€366.00
Please contact Customer Service for Availability
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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
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H G Bauernschmitt et al.
Biochimica et biophysica acta, 1150(1), 25-34 (1993-07-25)
In isolated inner medullary collecting duct (IMCD) cells requirements for the organic osmolyte glycerophosphorylcholine (GPC) vary with extracellular osmolality. To investigate mechanisms of osmotic adaptation GPC metabolism was studied under different osmotic conditions. In contrast to the GPC precursors choline
J Mitra et al.
International journal of andrology, 15(4), 345-354 (1992-08-01)
The functional interaction of the estrogen-induced uterine enzyme glycerylphosphorylcholine (GPC) diesterase with epididymal rat sperm before and after incubation under capacitating conditions was investigated indirectly, by measuring the glycerol phosphate (GP) released on enzymatic hydrolysis of GPC and using oxygen
D E Sok et al.
Neurochemical research, 20(2), 151-157 (1995-02-01)
Inhibition of a Zn(2+)-glycerophosphocholine cholinephosphodiesterase by thiols or tellurites were examined mechanistically. Inactivation of the phosphodiesterase by thio-carboxylates, which was due to the removal of Zn2+ in the catalytic site, was enhanced by introduction of an amino group in the
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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