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EC Tree
The taxonomic range for the selected organisms is: Bos taurus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lp-pla2, lipoprotein-associated phospholipase a2, paf acetylhydrolase, acetylhydrolase, plasma paf-ah, platelet-activating factor acetylhydrolase, paf-acetylhydrolase, pla2g7, lppla2, pafah,
more
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1-alkyl-2-acetyl-sn-glycero-3-phosphocholine: acetylhydrolase
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1-alkyl-2-acetylglycerophosphocholine esterase
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1-alkyl-2-acetyllecithin deacetylase
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1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase
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2-acetyl-1-alkylglycerophosphocholine esterase
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alkylacetyl-GPC:acetylhydrolase
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blood platelet-activating factor-acetyl hydrolase
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deacetylase, 1-alkyl-2-acetyllecithin
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LDL-associated phospholipase A2
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Lissencephaly-1 protein
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PAF 2-acylhydrolase
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phosphatide 2-acylhydrolase
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platelet activating factor acetylhydrolase
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platelet activating factor-acetylhydrolase
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platelet-activating factor acetylhydrolase
platelet-activating factor acetylhydrolyase
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Serine dependent phospholipase A2
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PAF acetylhydrolase
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PAF-acetylhydrolase
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PAF-AH
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platelet-activating factor acetylhydrolase
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platelet-activating factor acetylhydrolase
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platelet-activating factor acetylhydrolase
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1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
mechanism
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1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Arg29 and Arg22 in the one monomer contribute to the catalytic competence of the active site across the dimer interface, and complement the catalytic triad of Ser47, Asp192, and His195 in the second monomer
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hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
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hydrolysis of carboxylic ester
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1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
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1-hexadecyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-hexadecyl-sn-glycerol-3-phosphocholine + acetate
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i.e. PAF
-
?
1-hexadecyl-2-butyryl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + butanoate
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-
-
?
1-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + glutarate
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-
?
1-hexadecyl-2-propionyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + propionate
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-
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?
1-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + succinate
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-
-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid + H2O
1-O-alkyl-sn-glycero-3-phosphoric acid + acetate
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preferred substrate for the alpha1/alpha1 homodimer and the alpha1/alpha2 heterodimer
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
acetylated platelet-activation factor + H2O
?
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?
oxidized phospholipids + H2O
?
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protection against toxic effects of oxidized phospholipids
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-
?
additional information
?
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1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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-
-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. PAF
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. PAF
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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preferred substrate for alpha2/alpha2 homodimer of brain isoform I
-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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regulation of platelet-activating factor, protection against toxic effects of platelet-activating factor
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-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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platelet-activating factor
lyso-platelet-activating factor
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
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the substrate is a potent inflammatory mediator
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-
?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. platelet-activation factor
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. platelet-activation factor
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. platelet-activation factor
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
i.e. platelet-activation factor
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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biological inactivation of the platelet-activation factor by hydrolysis of the acetyl group at sn-2 position which is essential for activity of PAF
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?
additional information
?
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no activity against phosphatidylcholine or phosphatidylethanolamine, but hydrolysis of a phosphatidylcholine with an oxidatively fragmented acyl chain at the sn-2 position
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?
additional information
?
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substrate specificity, mammalian isozyme II possesses transacetylase activity as well
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?
additional information
?
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enzyme plays a critical role in control of neuronal migration during cortex development
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?
additional information
?
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enzyme plays a critical role in control of neuronal migration during cortex development
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?
additional information
?
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one of the physiological roles of isozyme II is to diversify the biological function of PAF by producing different lipid mediators such as analogues of PAF and C2-ceramide, mutations of the gene encoding the enzyme lead to severe diseases, e.g. brain impairment, mental retardation, or lymphoma development
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?
additional information
?
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selectively hydrolyzes oxidatively modified phosphatidylcholine. The purified enzyme does not degrade phospholipids with a long chain fatty acyl group at the sn-2 position
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?
additional information
?
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selectively hydrolyzes oxidatively modified phosphatidylcholine. The purified enzyme does not degrade phospholipids with a long chain fatty acyl group at the sn-2 position
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?
additional information
?
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PAF-like oxidatively fragmented phospholipids produced during oxidative stress
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?
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1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
oxidized phospholipids + H2O
?
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protection against toxic effects of oxidized phospholipids
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?
additional information
?
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1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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regulation of platelet-activating factor, protection against toxic effects of platelet-activating factor
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
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platelet-activating factor
lyso-platelet-activating factor
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
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?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
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the substrate is a potent inflammatory mediator
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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i.e. platelet-activation factor
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?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
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biological inactivation of the platelet-activation factor by hydrolysis of the acetyl group at sn-2 position which is essential for activity of PAF
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?
additional information
?
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enzyme plays a critical role in control of neuronal migration during cortex development
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?
additional information
?
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enzyme plays a critical role in control of neuronal migration during cortex development
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?
additional information
?
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one of the physiological roles of isozyme II is to diversify the biological function of PAF by producing different lipid mediators such as analogues of PAF and C2-ceramide, mutations of the gene encoding the enzyme lead to severe diseases, e.g. brain impairment, mental retardation, or lymphoma development
-
?
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Ca2+
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influences the dimerization of the enzyme
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5,5'-dithiobis(2-nitrobenzoate)
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diisopropylfluorophosphate
p-bromophenacyl bromide
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intracellular enzyme form Ib from brain
phenylmethylsulfonyl fluoride
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diisopropylfluorophosphate
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intracellular enzyme form Ib from brain
diisopropylfluorophosphate
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additional information
no inactivation by NaF or dithiothreitol
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additional information
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no inactivation by NaF or dithiothreitol
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0.0876
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine
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0.082 - 0.206
acetylated platelet-activation factor
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additional information
additional information
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kinetics
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0.082
acetylated platelet-activation factor
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mutant T103S, pH 7.4, 37°C
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0.092
acetylated platelet-activation factor
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mutant L48A, pH 7.4, 37°C
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0.135
acetylated platelet-activation factor
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mutant L194A, pH 7.4, 37°C
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0.206
acetylated platelet-activation factor
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wild-type enzyme, pH 7.4, 37°C
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1.45
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intracellular enzyme form Ib from brain
7.2
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cytosolic isoform II from liver
additional information
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-
additional information
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0.1309 U/ml, early puerperium
additional information
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0.1309 U/ml, late puerperium
additional information
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0.1418 U/ml, dry period
additional information
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0.1827 U/ml, mid-lactation
additional information
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0.2177 U/ml, second trimester of pregnancy
additional information
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0.2345 U/ml, first trimester of pregnancy
additional information
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0.2345 U/ml, lactation, infertility
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7
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intracellular enzyme forms from brain
7.4
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assay at
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additional information
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brenda
gamma-subunit and beta-subunit
Uniprot
brenda
german Holstein heifers
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brenda
Holstein-Frisian dairy cow
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brenda
isoform Ib
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brenda
isozyme Ib
Uniprot
brenda
isozymes I and II
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brenda
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brenda
the greatest PAF-AH activity is detected on the day of parturition (day 0), after which its activity dramatically decreases and by day 5, the enzyme activity is less than 7% of the level at parturition
brenda
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isozyme in endometrium is of the plasma enzyme type, enzyme activity decreases on day 20 in pregnant cows compared to cyclic cows on the same day, which show no changes in enzyme activity level
brenda
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brenda
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brenda
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brenda
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plasma isozyme
brenda
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brenda
additional information
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distribution of hetero- and homdimer of the alpha-subunit
brenda
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brenda
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brenda
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isoform Ib
brenda
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neonatal and adult, isozyme I
brenda
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brenda
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isozyme II
brenda
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brain enzyme
brenda
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isozyme II
brenda
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brenda
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isozyme II
brenda
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-
brenda
-
brenda
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PAFA_BOVIN
444
0
50133
Swiss-Prot
Secretory Pathway (Reliability: 1 )
PA1B2_BOVIN
229
0
25569
Swiss-Prot
other Location (Reliability: 1 )
PA1B3_BOVIN
232
0
25865
Swiss-Prot
other Location (Reliability: 1 )
PAFA2_BOVIN
392
0
43865
Swiss-Prot
other Location (Reliability: 3 )
Q1RML9_BOVIN
444
0
50151
TrEMBL
Secretory Pathway (Reliability: 1 )
V6F7P3_BOVIN
229
0
25569
TrEMBL
other Location (Reliability: 1 )
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100000
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intracellular enzyme form Ib from brain, gel filtration
26000
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isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit
29000
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1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
30000
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1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
43000
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1 * 43000, SDS-PAGE
40000
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isoform II from liver, gel filtration
40000
-
x * 40000, isozyme II, SDS-PAGE
45000
1 * 45000, SDS-PAGE
45000
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1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
45000
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isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit
45000
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x * 45000, plasma and endometrial enzyme, SDS-PAGE
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?
1 * 45000, SDS-PAGE
?
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x * 40000, isozyme II, SDS-PAGE
?
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x * 45000, plasma and endometrial enzyme, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
monomer
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1 * 60000, plasma enzyme SDS-PAGE
trimer
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1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
trimer
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the enzyme consists of two catalytic subunits alpha1 and alpha2 which form a catalytic dimer and a non-catalytic subunit beta. In addition the enzyme can aggregate to homodimers consisting of alpha1/alpha1 or alpha2/alpha2. The three forms differ in substrate specificity. The beta subunit accelerates the activity of the alpha2/alpha2 homodimer, suppresses the activity of the alpha1/alpha1 homodimer and has little influence on the activity of the alpha1/alpha2 heterodimer
trimer
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isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit
additional information
-
determination of structure-function relationship, dimerization of the brain isozyme is essential for both catalytic activity and stability, the monomeric enzyme is unstable, the alpha1 and alpha2 are catalytic subunits, the beta-subunit is a regulatory one
additional information
-
isozyme I exists of alpha1 and alpha2 subunits, catalytic subunits, tertiary structure, as well as of a beta-subunit, the beta-subunit is a regulatory one, isozyme II is a monomer
additional information
the enzyme exists as a trimer of a beta-subunit and a dimer of alpha-subunits, which can consist of a homodimer of 2 alpha1 or 2 alpha2-subunits or of a alpha1/alpha2 heterodimer
additional information
-
the enzyme exists as a trimer of a beta-subunit and a dimer of alpha-subunits, which can consist of a homodimer of 2 alpha1 or 2 alpha2-subunits or of a alpha1/alpha2 heterodimer
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additional information
-
isozyme II contains a myristoylation signal at the N-terminus
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12 mg/ml purified recombinant alpha1/alpha2 heterodimer, hanging-drop vapour diffusion method, 21°C, 17% PEG-MME 2000, 0.1 M sodium acetate, pH 6.4, 10 mM CaCl2, X-ray diffraction structure determination and analysis at resolution 2.1 A
crystal structure determination and analysis of the alpha1 subunit in complex with acetate at 1.7 A resolution
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purified recombinant R22K mutant, X-ray structure determination at 1.2 A resolution
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D20N
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site-directed mutagenesis, mutant is not efficiently expressed
D20R
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site-directed mutagenesis, mutant is not efficiently expressed
H149R
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brain isoform I, beta subunit, mutant has no ability to associate with the catalytic alpha-complexes
L194A
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site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
L26A
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site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
L48A
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site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
R22E
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site-directed mutagenesis, mutant is not efficiently expressed
R22K
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site-directed mutagenesis, inactive mutant
R29K
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site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
T103S
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site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
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47.5
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unfolding and irreversible denaturation at pH 9.5
52.3
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unfolding and irreversible denaturation at pH 6.5
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stable to several cycles of freezing and thawing
-
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cytosolic isoform II from liver
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from endometrium and plasma
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His-tagged alpha1/alpha2 heterodimer or alpha1 homodimer as maltose-binding fusion proteins from Escherichia coli XL1-Blue, removal of tags
intracellular enzyme from brain, isoform Ib
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isozyme II from liver, and isozyme I from brain
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active enzyme expressed in HEK 293 cells
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brain isoform I, expression of alpha1 and alpha2 subunits in Escherichia coli, expression of the beta subunit in Sf9 cells
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expression of the alpha1/alpha2 heterodimer or alpha1 homodimer as His-tagged maltose-binding fusion protein in Escherichia coli XL1-Blue using a bi-citronic expression vector
expression of the catalytic subunit alpha1-homodimer and alpha1-alpha2-heterodimer in Escherichia coli as GST-fusion protein, expression of wild-type and mutant enzymes as GST-fusion proteins in Escherichia coli
-
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medicine
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the gene for the beta subunit of brain enzyme isoform I is identical to a causative gene for Miller-Dieker lissencephaly
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Hattori, M.; Inoue, K.
Purification and characterization of bovine brain platelet-activating factor acetylhydrolase
J. Biol. Chem.
268
18748-18753
1993
Bos taurus
brenda
Hattori, K.; Hattori, M.; Adachi, H.; Tsujimoto, M.; Arai, H.; Inoue, K.
Purification and characterization of platelet-activating factor acetylhydrolase II from bovine liver cytosol
J. Biol. Chem.
270
22308-22313
1995
Bos taurus
brenda
Hough, S.R.; Parks, J.E.
Partial purification and localization of platelet-activating factor acetylhydrolase from bovine seminal plasma
J. Androl.
18
540-548
1997
Bos taurus
brenda
Maya, H.; Aoki, J.; Kato, H.; Ishii, J.; Hino, S.; Arai, H.; Inoue, K.
Biochemical characterization of various catalytic complexes of the brain platelet-activating factor acetylhydrolase
J. Biol. Chem.
274
31827-31832
1999
Bos taurus
brenda
Arai, H.; Koizumi, H.; Aoki, J.; Inoue, K.
Platelet-activating factor acetylhydrolase (PAF-AH)
J. Biochem.
131
635-640
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Tiemann, U.; Tomek, W.; Schneider, F.; Wollenhaupt, K.; Kanitz, W.; Becker, F.; Pohland, R.; Alm, H.
Platelet-activating factor (PAF)-like activity, localization of PAF receptor (PAF-R) and PAF-acetylhydrolase (PAF-AH) activity in bovine endometrium at different stages of the estrous cycle and early pregnancy
Prostaglandins
65
125-141
2001
Bos taurus
brenda
McMullen, T.W.; Li, J.; Sheffield, P.J.; Aoki, J.; Martin, T.W.; Arai, H.; Inoue, K.; Derewenda, Z.S.
The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib)
Protein Eng.
13
865-871
2000
Bos taurus
brenda
Sheffield, P.J.; McMullen, T.W.; Li, J.; Ho, Y.S.; Garrard, S.M.; Derewenda, U.; Derewenda, Z.S.
Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib
Protein Eng.
14
513-519
2001
Bos taurus (Q29460), Bos taurus
brenda
Lee, E.; Lee, S.J.; Lee, T.Y.; Chang, H.W.
cDNA cloning and expression of biologically active platelet activating factor-acetylhydrolase (PAF-AH) from bovine mammary gland
Biol. Pharm. Bull.
28
580-583
2005
Bos taurus
brenda
Moon, T.C.; Son, S.Y.; Chang, H.W.
Purification and characterization of 45 kDa PAF acetylhydrolase from bovine colostrum
Biol. Pharm. Bull.
30
1668-1673
2007
Bos taurus (Q29460 and P68401), Bos taurus
brenda
Turk, R.; Juretic, D.; Geres, D.; Bacic, G.; Milesevic, M.; Flegar-Mestric, Z.; Turk, N.; Svetina, A.
Bovine platelet-activating factor acetylhydrolase (PAF-AH) activity related to fertility
Anim. Reprod. Sci.
105
344-353
2008
Bos taurus
brenda