BRENDA - Enzyme Database
show all sequences of 3.1.4.50

Enzymatic properties of phosphatidylinositol-glycan-specific phospholipase C from rat liver and phosphatidylinositol-glycan-specific phospholipase D from rat serum [published erratum appears in Eur J Biochem 1991 Sep 15;200(3):812]

Stieger, S.; Diem, S.; Jakob, A.; Brodbeck, U.; Eur. J. Biochem. 197, 67-73 (1991)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
higher activity at low ionic strength, increasing amounts of NaCl, KCl, Na2SO4 or sodium phosphate decrease activity
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
Ca2+ does not protect
Rattus norvegicus
2,2'-dipyridyl
Ca2+ does not protect
Rattus norvegicus
Ca2+
slight decrease of activity above 1 mM, activation at 0.0001-0.01 mM
Rattus norvegicus
additional information
no inhibition by 1,7-phenanthroline or 2,2'-dipyridyl
Rattus norvegicus
NaHCO3
kinetics, pH-dependent: at pH 7.5, not at pH 5.5, reversible
Rattus norvegicus
NaOCN
kinetics, pH-dependent, reversible
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0001
-
phosphatidylinositol-glycan-anchor of membrane form of acetylcholinesterase
37°C, pH 7.4
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Rattus norvegicus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activation; large increase of activity between 0.0001 and 0.01 mM, slight decrease above 1 mM
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
Rattus norvegicus
isolated from bovine erythrocyte membranes
soluble acetylcholinesterase + phosphatidic acid
-
Rattus norvegicus
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
serum
-
Rattus norvegicus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
isolated from bovine erythrocyte membranes
646474
Rattus norvegicus
soluble acetylcholinesterase + phosphatidic acid
-
646474
Rattus norvegicus
-
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
isolated from bovine erythrocyte membranes
646474
Rattus norvegicus
soluble acetylcholinesterase + phosphatidic acid
-
646474
Rattus norvegicus
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
higher activity at low ionic strength, increasing amounts of NaCl, KCl, Na2SO4 or sodium phosphate decrease activity
Rattus norvegicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
7
about 60% of maximal activity at pH 5 and about half-maximal activity at pH 7, no activity above pH 8.5
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
higher activity at low ionic strength, increasing amounts of NaCl, KCl, Na2SO4 or sodium phosphate decrease activity
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
Ca2+ does not protect
Rattus norvegicus
2,2'-dipyridyl
Ca2+ does not protect
Rattus norvegicus
Ca2+
slight decrease of activity above 1 mM, activation at 0.0001-0.01 mM
Rattus norvegicus
additional information
no inhibition by 1,7-phenanthroline or 2,2'-dipyridyl
Rattus norvegicus
NaHCO3
kinetics, pH-dependent: at pH 7.5, not at pH 5.5, reversible
Rattus norvegicus
NaOCN
kinetics, pH-dependent, reversible
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0001
-
phosphatidylinositol-glycan-anchor of membrane form of acetylcholinesterase
37°C, pH 7.4
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Rattus norvegicus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activation; large increase of activity between 0.0001 and 0.01 mM, slight decrease above 1 mM
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
Rattus norvegicus
isolated from bovine erythrocyte membranes
soluble acetylcholinesterase + phosphatidic acid
-
Rattus norvegicus
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
serum
-
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
isolated from bovine erythrocyte membranes
646474
Rattus norvegicus
soluble acetylcholinesterase + phosphatidic acid
-
646474
Rattus norvegicus
-
phosphatidylinositol-glycan-anchored membrane form of acetylcholinesterase + H2O
isolated from bovine erythrocyte membranes
646474
Rattus norvegicus
soluble acetylcholinesterase + phosphatidic acid
-
646474
Rattus norvegicus
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
higher activity at low ionic strength, increasing amounts of NaCl, KCl, Na2SO4 or sodium phosphate decrease activity
Rattus norvegicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
7
about 60% of maximal activity at pH 5 and about half-maximal activity at pH 7, no activity above pH 8.5
Rattus norvegicus
Other publictions for EC 3.1.4.50
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749536
Masuda
Impact of glycosylphosphatidy ...
Homo sapiens, Mus musculus, Rattus norvegicus
Am. J. Physiol. Endocrinol. Metab.
316
E239-E250
2019
-
3
-
-
-
-
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6
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3
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3
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3
-
-
-
-
-
-
-
-
-
-
-
-
3
3
3
3
-
-
749993
Ritorto
Regulation of glycosylphospha ...
Homo sapiens, Mus musculus
Biol. Chem.
397
1147-1162
2016
-
2
-
-
-
-
-
-
-
-
-
-
-
4
-
-
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-
-
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-
-
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2
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-
-
-
-
-
-
-
-
-
-
-
751919
Jin
Phosphatidylinositol-glycan-p ...
Homo sapiens, Mus musculus
PLoS ONE
10
e0122120
2015
-
2
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
2
-
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2
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
729848
Lindqvist
Plasma glycosylphosphatidylino ...
Homo sapiens
Int. J. Clin. Exp. Med.
5
306-309
2012
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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1
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-
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1
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-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
709821
Raikwar
Glycosylphosphatidylinositol-s ...
Mus musculus, Mus musculus C57BL/6
Metab. Clin. Exp.
59
1413-1420
2010
-
-
1
-
-
-
-
-
-
-
-
-
-
141
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
691854
Jian-Hua
Important roles of glycosylpho ...
Homo sapiens
Clin. Biochem.
42
400-407
2009
-
-
1
-
-
-
-
-
-
-
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-
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2
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3
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2
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1
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3
-
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2
-
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-
-
-
-
-
-
693991
Gray
Plasma glycosylphosphatidylino ...
Homo sapiens
Metab. Clin. Exp.
57
473-478
2008
-
2
-
-
-
1
-
-
1
-
-
-
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2
-
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-
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5
-
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1
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2
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1
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1
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-
-
-
-
-
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5
-
-
1
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
680838
Watanabe
Growth factor induction of Cri ...
Homo sapiens
J. Biol. Chem.
282
31643-31655
2007
-
-
-
-
-
-
1
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-
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1
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1
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1
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-
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-
681720
Song
Role of glycosylphosphatidylin ...
Homo sapiens
Leuk. Res.
31
1701-1707
2007
-
-
-
-
-
-
1
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1
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1
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1
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1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681749
Song
How Glycosylphosphatidylinosit ...
Homo sapiens
Med. Hypotheses
69
660-665
2007
-
-
-
-
-
-
1
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-
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1
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2
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-
682945
Deeg
Statin therapy reduces serum l ...
Homo sapiens
Transl. Res.
150
153-157
2007
-
-
-
-
-
-
-
-
-
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2
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2
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663590
Raikwar
Glycosylphosphatidylinositol-s ...
Mus musculus
Am. J. Physiol.
290
E463-470
2006
-
-
-
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1
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2
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1
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1
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-
664499
Naghibalhossaini
Evidence for CEA release from ...
Homo sapiens
Cancer Lett.
234
158-167
2006
1
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
-
-
-
5
-
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1
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1
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1
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1
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5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668244
Bonilla
Phospholipase cleavage of D- a ...
Bos taurus
Chem. Eur. J.
12
1513-1528
2006
-
-
-
-
-
-
-
-
-
-
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3
-
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1
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6
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1
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6
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-
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-
669623
Chalasani
Glycosylphosphatidylinositol-s ...
Homo sapiens
J. Clin. Endocrinol. Metab.
91
2279-2285
2006
-
-
-
-
-
-
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-
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1
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2
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-
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1
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1
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1
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-
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-
679322
Yoshida
-
Cleavage with phospholipase of ...
Bos taurus
Comp. Biochem. Physiol. B
143B
138-144
2006
-
-
-
-
-
-
1
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1
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681627
Elortza
Modification-specific proteomi ...
Bos taurus
J. Proteome Res.
5
935-943
2006
-
-
-
-
-
-
-
-
-
-
-
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1
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1
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2
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1
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2
-
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-
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-
663876
Yamamoto
Cleavage of carcinoembryonic a ...
Homo sapiens
Biochem. Biophys. Res. Commun.
333
223-229
2005
-
-
-
-
-
-
-
-
-
-
-
1
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2
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1
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2
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1
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1
-
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2
-
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-
-
-
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-
-
-
-
-
-
-
-
-
663968
Raikwar
Mutating His29, His125, His133 ...
Mus musculus
Biochem. J.
391
285-289
2005
-
-
1
-
6
-
-
-
-
-
-
-
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2
-
1
-
-
-
-
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1
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6
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1
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-
-
-
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-
-
-
-
-
-
-
-
-
664464
Gregory
GPI-specific phospholipase D ( ...
Mus musculus
Bone
37
139-147
2005
-
-
-
-
-
-
-
-
1
-
-
1
-
3
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
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Effect of glycosylphosphatidyl ...
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Homo sapiens
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Insulin reduces serum glycosyl ...
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646475
Bowen
Glucose and insulin regulate g ...
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2001
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Down-regulation of glycosylpho ...
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646486
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Glycosylphosphatidylinositol-s ...
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Regulation of brain glycosylph ...
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Glycosylphosphatidylinositol-s ...
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Tsujioka
Intracellular cleavage of glyc ...
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Enzymatic release of Zn2+-glyc ...
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Tsujioka
Posttranslational modification ...
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646494
LeBoeuf
Mouse glycosylphosphatidylinos ...
Mus musculus
Mamm. Genome
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Hari
Uptake and intracellular stabi ...
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Kueng
Expression of intracellular an ...
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Stadelmann
The C-terminus of glycosylphos ...
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Biochim. Biophys. Acta
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1997
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Maguire
Glycosyl phosphatidyl inositol ...
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A phospholipase D specific for ...
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