BRENDA - Enzyme Database
show all sequences of 2.7.8.15

Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast

Sharma, C.B.; Lehle, L.; Tanner, W.; Eur. J. Biochem. 126, 319-325 (1982)

Data extracted from this reference:

General Stability
General Stability
Organism
a 1:4 dilution leads to a 65% loss of activity
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
tunicamycin
1 mM, complete inhibition
Saccharomyces cerevisiae
UDP
1 mM, 55% inhibition
Saccharomyces cerevisiae
UMP
1 mM, 45% inhibition
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
dolichyl phosphate
pH 7.5
Saccharomyces cerevisiae
0.015
-
UDP-GlcNAc
pH 7.5
Saccharomyces cerevisiae
0.18
-
dolichyl phosphate
pH 7.5
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Saccharomyces cerevisiae
16020
-
microsome
-
Saccharomyces cerevisiae
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
divalent metal required, Ca2+ is less effective than Mg2+
Saccharomyces cerevisiae
Mg2+
divalent metal required, optimal activity in presence of Mg2+
Saccharomyces cerevisiae
Mn2+
divalent metal required, Mn2+ is less effective than Mg2+
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
Saccharomyces cerevisiae
first enzyme of dolichol pathway
?
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
Saccharomyces cerevisiae X2180-1A
first enzyme of dolichol pathway
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
X2180-1A
-
Saccharomyces cerevisiae X2180-1A
-
X2180-1A
-
Storage Stability
Storage Stability
Organism
-20C, solubilized enzyme loses 96% of its activity after 6 days, only 20% loss of activity after 6 days in presence of 0.07 mM UDP-GlcNAc
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
-
645348
Saccharomyces cerevisiae
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
645348
Saccharomyces cerevisiae
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
-
645348
Saccharomyces cerevisiae X2180-1A
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
645348
Saccharomyces cerevisiae X2180-1A
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
first enzyme of dolichol pathway
645348
Saccharomyces cerevisiae
?
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
first enzyme of dolichol pathway
645348
Saccharomyces cerevisiae X2180-1A
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Saccharomyces cerevisiae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
pH 6.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
Saccharomyces cerevisiae
General Stability (protein specific)
General Stability
Organism
a 1:4 dilution leads to a 65% loss of activity
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
tunicamycin
1 mM, complete inhibition
Saccharomyces cerevisiae
UDP
1 mM, 55% inhibition
Saccharomyces cerevisiae
UMP
1 mM, 45% inhibition
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
dolichyl phosphate
pH 7.5
Saccharomyces cerevisiae
0.015
-
UDP-GlcNAc
pH 7.5
Saccharomyces cerevisiae
0.18
-
dolichyl phosphate
pH 7.5
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Saccharomyces cerevisiae
16020
-
microsome
-
Saccharomyces cerevisiae
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
divalent metal required, Ca2+ is less effective than Mg2+
Saccharomyces cerevisiae
Mg2+
divalent metal required, optimal activity in presence of Mg2+
Saccharomyces cerevisiae
Mn2+
divalent metal required, Mn2+ is less effective than Mg2+
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
Saccharomyces cerevisiae
first enzyme of dolichol pathway
?
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
Saccharomyces cerevisiae X2180-1A
first enzyme of dolichol pathway
?
-
-
?
Storage Stability (protein specific)
Storage Stability
Organism
-20C, solubilized enzyme loses 96% of its activity after 6 days, only 20% loss of activity after 6 days in presence of 0.07 mM UDP-GlcNAc
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
-
645348
Saccharomyces cerevisiae
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
645348
Saccharomyces cerevisiae
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
-
645348
Saccharomyces cerevisiae X2180-1A
UMP + N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
645348
Saccharomyces cerevisiae X2180-1A
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
first enzyme of dolichol pathway
645348
Saccharomyces cerevisiae
?
-
-
-
?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate
first enzyme of dolichol pathway
645348
Saccharomyces cerevisiae X2180-1A
?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Saccharomyces cerevisiae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
8.5
pH 6.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
Saccharomyces cerevisiae
Other publictions for EC 2.7.8.15
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)
737859
Kim
The UDP-N-acetylglucosamine:do ...
Solanum tuberosum
Biosci. Biotechnol. Biochem.
77
1589-1592
2013
-
2
1
-
-
-
-
-
-
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3
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2
1
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-
703322
Bretthauer
Structure, expression, and reg ...
Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Curr. Drug Targets
10
477-482
2009
-
-
5
-
1
-
5
-
5
-
8
5
-
5
-
-
5
-
-
5
-
-
5
-
-
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-
-
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5
-
-
1
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5
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-
5
-
8
5
-
-
-
5
-
5
-
-
5
-
-
-
-
-
-
-
-
-
-
5
5
-
-
-
691880
Plante
Mucolipidosis II: a single cau ...
Homo sapiens
Clin. Genet.
73
236-244
2008
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
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1
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673891
Gao
Unexpected basis for impaired ...
Cricetulus griseus, Mesocricetus auratus
Glycobiology
18
125-134
2007
-
-
-
-
-
-
2
-
1
-
-
-
-
2
-
-
-
-
-
1
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3
-
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-
2
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-
1
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1
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
661252
Mendelsohn
A hypomorphic allele of the fi ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1723
33-44
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
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1
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1
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-
-
-
-
-
-
-
645357
Sorensen
Characterisation of the gptA g ...
Aspergillus niger, Aspergillus niger N402
Biochim. Biophys. Acta
1619
89-97
2003
-
-
1
-
-
-
-
-
-
-
1
2
-
6
-
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4
1
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1
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1
2
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4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
645362
Wu
Deficiency of UDP-GlcNAc: doli ...
Homo sapiens
Hum. Mutat.
22
144-150
2003
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
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2
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1
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-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
645363
Meissner
Regulation of UDP-N-acetylgluc ...
Mus musculus
Biochem. J.
338
561-568
1999
-
-
-
-
-
-
-
-
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-
1
-
3
-
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1
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2
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645360
Huang
Characterization of multiple t ...
Cricetulus griseus
Mol. Cell. Biochem.
181
97-106
1998
-
-
-
-
-
-
-
-
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3
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1
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1
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1
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1
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-
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-
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645361
Scocca
Aspartic acid 252 and asparagi ...
Cricetulus griseus
Glycobiology
7
1181-1191
1997
-
-
1
-
-
-
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-
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1
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2
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2
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645367
Dan
Oligomerization of hamster UDP ...
Cricetulus griseus
J. Biol. Chem.
272
14214-14219
1997
-
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-
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1
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-
2
-
1
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1
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1
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1
1
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1
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1
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1
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1
1
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645366
Dan
Hamster UDP-N-acetylglucosamin ...
Cricetulus griseus
J. Biol. Chem.
271
30717-30724
1996
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1
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645356
Zeng
UDP-N-acetylglucosamine:dolich ...
Glycine max
Eur. J. Biochem.
233
458-466
1995
2
-
-
-
-
-
4
-
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-
1
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-
2
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-
1
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1
1
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2
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2
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4
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1
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1
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1
1
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-
2
-
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-
-
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-
-
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-
645358
Kukuruzinska
Diminished activity of the fir ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1247
51-59
1995
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-
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1
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3
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645359
Mota
Developmental regulation and t ...
Cricetulus griseus
Biochem. Biophys. Res. Commun.
204
284-291
1994
-
-
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-
15
-
-
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1
1
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2
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7
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2
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15
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1
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7
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2
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645364
Zara
Role of the carboxyl terminus ...
Cricetulus griseus
J. Biol. Chem.
269
19108-19115
1994
-
-
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4
-
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1
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1
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1
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4
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1
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2
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645365
Rajput
Structure and organization of ...
Mus musculus
J. Biol. Chem.
269
9590-9597
1994
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1
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5
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1
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1
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1
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2
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645355
Chandra
Specific lipids enhance the ac ...
Rattus norvegicus
Arch. Biochem. Biophys.
290
345-354
1991
3
-
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-
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2
1
1
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1
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1
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1
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2
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3
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1
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645350
Shailubhai
Purification and characterizat ...
Bos taurus
J. Biol. Chem.
263
15964-15972
1988
1
-
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1
11
2
1
2
1
1
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2
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1
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1
1
1
2
1
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1
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1
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1
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11
-
2
1
2
1
1
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1
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1
1
1
2
1
-
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1
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-
-
-
-
-
-
-
645354
Kaushal
Properties of solubilized UDP- ...
Glycine max
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1986
2
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11
2
1
3
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1
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1
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1
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1
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2
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11
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2
1
3
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1
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1
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1
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645351
Kaushal
Purification and properties of ...
Sus scrofa
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6
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2
2
1
3
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2
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1
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2
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1
1
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1
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6
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2
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2
1
3
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1
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2
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1
1
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1
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645348
Sharma
Solubilization and characteriz ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180-1A
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-
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1
3
3
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3
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6
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1
4
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1
1
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1
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3
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3
2
3
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2
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1
4
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1
1
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645352
Plouhar
A phospholipid requirement for ...
Rattus norvegicus
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1
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1
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3
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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
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1
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645349
Villemez
Properties of a soluble polypr ...
Acanthamoeba castellanii
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-
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1
2
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2
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1
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1
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1
1
1
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1
1
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1
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2
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2
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2
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2
1
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1
1
1
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1
1
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645353
Heifetz
Mechanism of action of tunicam ...
Sus scrofa
Biochemistry
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2186-2192
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1
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1
2
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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