PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
29132308-0	2017	Effect of two non-synonymous ecto-5"-nucleotidase variants on the genetic architecture of inosine 5"-monophosphate (IMP) and its degradation products in Japanese Black beef.	Inosine Monophosphate	90-114	5'-nucleotidase	Bos taurus	29-49
29132308-0	2017	Effect of two non-synonymous ecto-5"-nucleotidase variants on the genetic architecture of inosine 5"-monophosphate (IMP) and its degradation products in Japanese Black beef.	Inosine Monophosphate	116-119	5'-nucleotidase	Bos taurus	29-49
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine Monophosphate	105-108	5'-nucleotidase	Bos taurus	4-24
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine Monophosphate	105-108	5'-nucleotidase	Bos taurus	26-30
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine Monophosphate	105-108	5'-nucleotidase	Bos taurus	63-67
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine	112-119	5'-nucleotidase	Bos taurus	4-24
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine	112-119	5'-nucleotidase	Bos taurus	26-30
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	Inosine	112-119	5'-nucleotidase	Bos taurus	63-67
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	bta9	164-168	5'-nucleotidase	Bos taurus	4-24
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	bta9	164-168	5'-nucleotidase	Bos taurus	26-30
29132308-9	2017	The ecto-5"-nucleotidase (NT5E) gene, which encodes the enzyme NT5E for the extracellular degradation of IMP to inosine, was located near the significant region on BTA9.	bta9	164-168	5'-nucleotidase	Bos taurus	63-67
11173996-0	2001	Adenosine diphosphate ribose dilates bovine coronary small arteries through apyrase- and 5"-nucleotidase-mediated metabolism.	Adenosine Diphosphate Ribose	0-28	5'-nucleotidase	Bos taurus	89-104
28242355-1	2017	The enzymatic activities of NTPDase, 5"-nucleotidase and adenosine deaminase (ADA) are important in regulating the concentration of adenine nucleotides, molecules known to be involved on platelet aggregation.	Adenine Nucleotides	132-151	5'-nucleotidase	Bos taurus	37-52
28242355-3	2017	Taking into consideration the association between the purinergic system and hemostasis, this study aimed to evaluate the enzymatic activities of NTPDase (hydrolyze ATP and ADP), 5"-nucleotidase (hydrolyze AMP) and ADA (deamination of adenosine) in platelets from cattle experimentally infected by Fasciola hepatica on days 20, 40, 60 and 80 post-infection (PI).	Adenosine Monophosphate	205-208	5'-nucleotidase	Bos taurus	178-193
28242355-6	2017	Reduction of NTPDase (p < 0.05) hydrolysing ATP (days 20, 40 and 60 PI), and ADP (days 40, 60 and 80 PI), and on 5"-nucleotidase hydrolyzing AMP (days 40 and 60 PI) was observed.	Adenosine Monophosphate	144-147	5'-nucleotidase	Bos taurus	116-131
27589035-0	2017	Isonicotinohydrazones as inhibitors of alkaline phosphatase and ecto-5"-nucleotidase.	isonicotinohydrazones	0-21	5'-nucleotidase	Bos taurus	64-84
23691116-5	2013	The yeast cells harbouring cytosolic 5"-nucleotidase II displayed a shorter duplication time and a significant modification of purine and pyrimidine derivatives concentration as compared with the control strain.	purine	127-133	5'-nucleotidase	Bos taurus	37-52
23691116-5	2013	The yeast cells harbouring cytosolic 5"-nucleotidase II displayed a shorter duplication time and a significant modification of purine and pyrimidine derivatives concentration as compared with the control strain.	pyrimidine	138-148	5'-nucleotidase	Bos taurus	37-52
18404487-6	2006	The ecto-5" nucleotidase inhibitor alphabetamADP prevented the production adenosine by the apical membrane of the bovine RPE.	alphabetamadp	35-48	5'-nucleotidase	Bos taurus	4-24
18404487-6	2006	The ecto-5" nucleotidase inhibitor alphabetamADP prevented the production adenosine by the apical membrane of the bovine RPE.	Adenosine	74-83	5'-nucleotidase	Bos taurus	4-24
28504100-3	2017	Seric activities of NTPDase (ATP substrate), 5"-nucleotidase, and ADA were lower (P<0.05) in D. viviparus infected animals compared to uninfected cows.	seric	0-5	5'-nucleotidase	Bos taurus	45-60
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Cyclic AMP	18-22	5'-nucleotidase	Bos taurus	239-259
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Adenosine	23-32	5'-nucleotidase	Bos taurus	239-259
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Adenosine	75-84	5'-nucleotidase	Bos taurus	239-259
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Adenosine Monophosphate	19-22	5'-nucleotidase	Bos taurus	239-259
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Adenosine Monophosphate	98-101	5'-nucleotidase	Bos taurus	239-259
12724271-1	2003	The extracellular cAMP-adenosine pathway refers to the local production of adenosine mediated by cAMP egress into the extracellular space, conversion of cAMP to AMP by ectophosphodiesterase (PDE), and the metabolism of AMP to adenosine by ecto-5"-nucleotidase.	Adenosine	75-84	5'-nucleotidase	Bos taurus	239-259
11432867-1	2001	Cytosolic 5"-nucleotidase/phosphotransferase (cN-II), specific for purine monophosphates and their deoxyderivatives, acts through the formation of a phosphoenzyme intermediate.	purine monophosphates	67-88	5'-nucleotidase	Bos taurus	10-25
11173996-7	2001	The adenosine production was blocked by the 5"-nucleotidase inhibitor, alpha,beta-methylene adenosine 5"-diphosphate (MADP, 1 mmol/l), which was accompanied by a corresponding accumulation of 5"-AMP.	Adenosine	4-13	5'-nucleotidase	Bos taurus	44-59
11173996-7	2001	The adenosine production was blocked by the 5"-nucleotidase inhibitor, alpha,beta-methylene adenosine 5"-diphosphate (MADP, 1 mmol/l), which was accompanied by a corresponding accumulation of 5"-AMP.	alpha,beta-methyleneadenosine 5'-diphosphate	71-116	5'-nucleotidase	Bos taurus	44-59
11173996-7	2001	The adenosine production was blocked by the 5"-nucleotidase inhibitor, alpha,beta-methylene adenosine 5"-diphosphate (MADP, 1 mmol/l), which was accompanied by a corresponding accumulation of 5"-AMP.	alpha,beta-methyleneadenosine 5'-diphosphate	118-122	5'-nucleotidase	Bos taurus	44-59
11173996-7	2001	The adenosine production was blocked by the 5"-nucleotidase inhibitor, alpha,beta-methylene adenosine 5"-diphosphate (MADP, 1 mmol/l), which was accompanied by a corresponding accumulation of 5"-AMP.	Adenosine Monophosphate	192-198	5'-nucleotidase	Bos taurus	44-59
11173996-12	2001	We concluded that ADPR produces vasodilation in small coronary arteries and that the action of ADPR is associated with the adenosine production via an apyrase- and 5"-nucleotidase-mediated metabolism.	Adenosine	123-132	5'-nucleotidase	Bos taurus	164-179
11071366-0	2000	Oxidative inactivation of brain ecto-5"-nucleotidase by thiols/Fe2+ system.	Sulfhydryl Compounds	56-62	5'-nucleotidase	Bos taurus	32-52
11071366-0	2000	Oxidative inactivation of brain ecto-5"-nucleotidase by thiols/Fe2+ system.	ammonium ferrous sulfate	63-67	5'-nucleotidase	Bos taurus	32-52
11071366-1	2000	5"-Nucleotidase, responsible for the conversion of adenosine-5"-monophosphate into adenosine, was purified from bovine brain membranes, and subjected to oxidative inactivation.	adenosine-5"-monophosphate	51-77	5'-nucleotidase	Bos taurus	0-15
11071366-1	2000	5"-Nucleotidase, responsible for the conversion of adenosine-5"-monophosphate into adenosine, was purified from bovine brain membranes, and subjected to oxidative inactivation.	Adenosine	51-60	5'-nucleotidase	Bos taurus	0-15
11071366-2	2000	The 5"-nucleotidase activity decreased slightly after the exposure to either glutathione or Fe2+.	Glutathione	77-88	5'-nucleotidase	Bos taurus	4-19
11071366-2	2000	The 5"-nucleotidase activity decreased slightly after the exposure to either glutathione or Fe2+.	ammonium ferrous sulfate	92-96	5'-nucleotidase	Bos taurus	4-19
11071366-3	2000	The glutathione-mediated inactivation of 5"-nucleotidase was potentiated remarkably by Fe2+, but not Cu2+, in a concentration-dependent manner.	Glutathione	4-15	5'-nucleotidase	Bos taurus	41-56
11071366-3	2000	The glutathione-mediated inactivation of 5"-nucleotidase was potentiated remarkably by Fe2+, but not Cu2+, in a concentration-dependent manner.	ammonium ferrous sulfate	87-91	5'-nucleotidase	Bos taurus	41-56
11071366-3	2000	The glutathione-mediated inactivation of 5"-nucleotidase was potentiated remarkably by Fe2+, but not Cu2+, in a concentration-dependent manner.	cupric ion	101-105	5'-nucleotidase	Bos taurus	41-56
11071366-10	2000	Overall, thiols, expressing more inhibitory effect on the activity of 5"-nucleotidase, were found to be more effective in potentiating the Fe2+-mediated inactivation.	Sulfhydryl Compounds	9-15	5'-nucleotidase	Bos taurus	70-85
11071366-10	2000	Overall, thiols, expressing more inhibitory effect on the activity of 5"-nucleotidase, were found to be more effective in potentiating the Fe2+-mediated inactivation.	ammonium ferrous sulfate	139-143	5'-nucleotidase	Bos taurus	70-85
11071366-11	2000	Further, kinetic analyses indicate that Fe2+ and thiols inhibit the 5"-nucleotidase in a competitive or uncompetitive manner, respectively.	ammonium ferrous sulfate	40-44	5'-nucleotidase	Bos taurus	68-83
11071366-11	2000	Further, kinetic analyses indicate that Fe2+ and thiols inhibit the 5"-nucleotidase in a competitive or uncompetitive manner, respectively.	Sulfhydryl Compounds	49-55	5'-nucleotidase	Bos taurus	68-83
11071366-12	2000	These results suggest that ecto-5"-nucleotidase from brain membrane is one of proteins susceptible to thiols/Fe2+-catalyzed oxidation, and the oxidative inactivation may be related to the selective association of Fe2+ and thiols to the enzyme molecule.	Sulfhydryl Compounds	102-108	5'-nucleotidase	Bos taurus	27-47
11071366-12	2000	These results suggest that ecto-5"-nucleotidase from brain membrane is one of proteins susceptible to thiols/Fe2+-catalyzed oxidation, and the oxidative inactivation may be related to the selective association of Fe2+ and thiols to the enzyme molecule.	ammonium ferrous sulfate	109-113	5'-nucleotidase	Bos taurus	27-47
11071366-12	2000	These results suggest that ecto-5"-nucleotidase from brain membrane is one of proteins susceptible to thiols/Fe2+-catalyzed oxidation, and the oxidative inactivation may be related to the selective association of Fe2+ and thiols to the enzyme molecule.	ammonium ferrous sulfate	213-217	5'-nucleotidase	Bos taurus	27-47
11071366-12	2000	These results suggest that ecto-5"-nucleotidase from brain membrane is one of proteins susceptible to thiols/Fe2+-catalyzed oxidation, and the oxidative inactivation may be related to the selective association of Fe2+ and thiols to the enzyme molecule.	Sulfhydryl Compounds	222-228	5'-nucleotidase	Bos taurus	27-47
9687019-1	1998	Cytosolic 5"-nucleotidase, acting preferentially on IMP, GMP and their deoxyderivatives, endowed with phosphotransferase activity, is a widespread enzyme responsible for the regulation of intracellular IMP and GMP concentrations and the phosphorylation of purine nucleoside pro-drugs.	Inosine Monophosphate	52-55	5'-nucleotidase	Bos taurus	10-25
9834459-4	1998	Specific binding of [3H]progesterone overlapped with the distributions of 5"-nucleotidase and luteinizing hormone receptor (luteal cell surface membrane markers) in both control and digitonin-treated gradients at all stages of the luteal phase.	Digitonin	182-191	5'-nucleotidase	Bos taurus	74-89
9687019-1	1998	Cytosolic 5"-nucleotidase, acting preferentially on IMP, GMP and their deoxyderivatives, endowed with phosphotransferase activity, is a widespread enzyme responsible for the regulation of intracellular IMP and GMP concentrations and the phosphorylation of purine nucleoside pro-drugs.	guanosine 5'-monophosphorothioate	57-60	5'-nucleotidase	Bos taurus	10-25
9687019-1	1998	Cytosolic 5"-nucleotidase, acting preferentially on IMP, GMP and their deoxyderivatives, endowed with phosphotransferase activity, is a widespread enzyme responsible for the regulation of intracellular IMP and GMP concentrations and the phosphorylation of purine nucleoside pro-drugs.	Inosine Monophosphate	202-205	5'-nucleotidase	Bos taurus	10-25
9687019-1	1998	Cytosolic 5"-nucleotidase, acting preferentially on IMP, GMP and their deoxyderivatives, endowed with phosphotransferase activity, is a widespread enzyme responsible for the regulation of intracellular IMP and GMP concentrations and the phosphorylation of purine nucleoside pro-drugs.	guanosine 5'-monophosphorothioate	210-213	5'-nucleotidase	Bos taurus	10-25
8843796-5	1996	Activities of angiotensin-converting enzyme (ACE) and 5"-nucleotidase (NCT) were assayed in Earle"s balanced salts solution utilizing [3H]benzoyl-Phe-Ala-Pro ([3H]BPAP) and 5"-[14C]AMP as substrates, respectively.	earle"s balanced salts solution	92-123	5'-nucleotidase	Bos taurus	54-69
9277483-12	1997	In tandem with 5"-nucleotidase, it produces adenosine, a powerful vasodilator, especially in hypoxic or ischemic conditions that favor the release of ATP.	Adenosine	44-53	5'-nucleotidase	Bos taurus	15-30
9277483-12	1997	In tandem with 5"-nucleotidase, it produces adenosine, a powerful vasodilator, especially in hypoxic or ischemic conditions that favor the release of ATP.	Adenosine Triphosphate	150-153	5'-nucleotidase	Bos taurus	15-30
9185625-3	1997	The chiro-inositol contents in several different GPI-anchored proteins including 5"-nucleotidase of bovine liver and alkaline phosphatase of mouse NS-1 varied with hydrolytic conditions of these GPI anchor.	Inositol	10-18	5'-nucleotidase	Bos taurus	81-96
9185625-3	1997	The chiro-inositol contents in several different GPI-anchored proteins including 5"-nucleotidase of bovine liver and alkaline phosphatase of mouse NS-1 varied with hydrolytic conditions of these GPI anchor.	Glycosylphosphatidylinositols	49-52	5'-nucleotidase	Bos taurus	81-96
8142426-0	1994	Mutational analysis of the COOH-terminal hydrophobic domain of bovine liver 5"-nucleotidase as a signal for glycosylphosphatidylinositol (GPI) anchor attachment.	Glycosylphosphatidylinositols	108-136	5'-nucleotidase	Bos taurus	76-91
8760365-1	1996	Cytosolic 5"-nucleotidase preferentially catalysing the hydrolysis of IMP, GMP and their deoxy derivatives, and endowed with phosphotransferase activity, was purified from calf thymus and its reaction mechanism was studied.	Inosine Monophosphate	70-73	5'-nucleotidase	Bos taurus	10-25
8760365-1	1996	Cytosolic 5"-nucleotidase preferentially catalysing the hydrolysis of IMP, GMP and their deoxy derivatives, and endowed with phosphotransferase activity, was purified from calf thymus and its reaction mechanism was studied.	guanosine 5'-monophosphorothioate	75-78	5'-nucleotidase	Bos taurus	10-25
8142426-0	1994	Mutational analysis of the COOH-terminal hydrophobic domain of bovine liver 5"-nucleotidase as a signal for glycosylphosphatidylinositol (GPI) anchor attachment.	Glycosylphosphatidylinositols	138-141	5'-nucleotidase	Bos taurus	76-91
8142426-5	1994	In conclusion, the hydrophobicity of 13 amino acids in length was enough for the GPI modification of the bovine liver 5"-nucleotidase.	Glycosylphosphatidylinositols	81-84	5'-nucleotidase	Bos taurus	118-133
8081255-0	1994	Studies on the GPI-anchored enzyme, hepatic 5"-nucleotidase.	Glycosylphosphatidylinositols	15-18	5'-nucleotidase	Bos taurus	44-59
8305428-0	1994	Microheterogeneity in glycosylphosphatidylinositol anchor structures of bovine liver 5"-nucleotidase.	Glycosylphosphatidylinositols	22-50	5'-nucleotidase	Bos taurus	85-100
8305428-1	1994	In our study, 5"-nucleotidase was released from bovine liver by the treatment with Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and purified to a homogeneous state by concanavalin A-Sepharose and (diethylaminoethyl)-Toyopearl column chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sepharose	206-215	5'-nucleotidase	Bos taurus	14-29
8305428-1	1994	In our study, 5"-nucleotidase was released from bovine liver by the treatment with Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and purified to a homogeneous state by concanavalin A-Sepharose and (diethylaminoethyl)-Toyopearl column chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	(diethylaminoethyl)	220-239	5'-nucleotidase	Bos taurus	14-29
8081255-6	1994	The cleavage/attachment site of the GPI anchor in the C-terminal of 5"-nucleotidase was shown to be Ser523.	Glycosylphosphatidylinositols	36-39	5'-nucleotidase	Bos taurus	68-83
8305428-1	1994	In our study, 5"-nucleotidase was released from bovine liver by the treatment with Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and purified to a homogeneous state by concanavalin A-Sepharose and (diethylaminoethyl)-Toyopearl column chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	276-298	5'-nucleotidase	Bos taurus	14-29
8081255-8	1994	By site-directed mutagenesis, we determined the minimal length of the hydrophobic peptide to be 13 amino acids for expression of 5"-nucleotidase as a GPI-anchored form on the COS cell surface.	Glycosylphosphatidylinositols	150-153	5'-nucleotidase	Bos taurus	129-144
8305428-1	1994	In our study, 5"-nucleotidase was released from bovine liver by the treatment with Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and purified to a homogeneous state by concanavalin A-Sepharose and (diethylaminoethyl)-Toyopearl column chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	299-313	5'-nucleotidase	Bos taurus	14-29
2169262-1	1990	Alkaline phosphatase and 5"-nucleotidase are covalently linked to phosphatidylinositol in bovine fat globule membrane, as demonstrated by their release following treatment with phospholipase C specific for phosphatidylinositol.	Phosphatidylinositols	66-86	5'-nucleotidase	Bos taurus	25-40
8305428-2	1994	Purified 5"-nucleotidase were then cleaved by cyanogen bromide (CNBr), and then inositol phosphoglycan-containing C-terminal peptides (IPG peptides) were separated by C18 reverse-phase liquid chromatography and analyzed by peptide sequencer, amino acid analyzer, gas chromatography (GC), and GC-mass spectrometry (MS).	2-Isopropoxyethanol	135-138	5'-nucleotidase	Bos taurus	9-24
8361957-0	1993	Selective extraction of alkaline phosphatase and 5"-nucleotidase from milk fat globule membranes by a single phase n-butanol procedure.	1-Butanol	115-124	5'-nucleotidase	Bos taurus	49-64
8361957-2	1993	For 5"-nucleotidase, higher n-butanol concentrations lead to loss of activity, while lower concentrations were ineffective in extracting the enzyme.	1-Butanol	28-37	5'-nucleotidase	Bos taurus	4-19
8361957-3	1993	When extractions were performed at 0 degrees C, similar yields were obtained for alkaline phosphatase extraction with 8% (v/v) n-butanol, but 5"-nucleotidase extraction required 10% (v/v) n-butanol for similar yields.	1-Butanol	188-197	5'-nucleotidase	Bos taurus	142-157
8361957-4	1993	However, 5"-nucleotidase was less susceptible to denaturation during extraction at 0 degrees C. The Km values and substrate specificities for both alkaline phosphatase and 5"-nucleotidase were unchanged by extraction with 8% (v/v) n-butanol.	1-Butanol	231-240	5'-nucleotidase	Bos taurus	172-187
8340354-1	1993	A glycosylphosphatidylinositol (GPI)-anchored protein, 5"-nucleotidase [EC 3.1.3.5], was released from the membrane of bovine liver by use of phosphatidylinositol-specific phospholipase C (PI-PLC) of Bacillus thuringiensis and purified by several column chromatographies to a homogeneous state.	Glycosylphosphatidylinositols	2-30	5'-nucleotidase	Bos taurus	55-70
8340354-1	1993	A glycosylphosphatidylinositol (GPI)-anchored protein, 5"-nucleotidase [EC 3.1.3.5], was released from the membrane of bovine liver by use of phosphatidylinositol-specific phospholipase C (PI-PLC) of Bacillus thuringiensis and purified by several column chromatographies to a homogeneous state.	Glycosylphosphatidylinositols	32-35	5'-nucleotidase	Bos taurus	55-70
1864447-0	1991	Differential theophylline inhibition of alkaline phosphatase and 5"-nucleotidase of bovine milk fat globule membranes.	Theophylline	13-25	5'-nucleotidase	Bos taurus	65-80
1864447-6	1991	The 5"-nucleotidase activity was resistant to theophylline inhibition with 50% inhibition produced by 33.9 +/- 3.1 mM theophylline.	Theophylline	46-58	5'-nucleotidase	Bos taurus	4-19
1864447-6	1991	The 5"-nucleotidase activity was resistant to theophylline inhibition with 50% inhibition produced by 33.9 +/- 3.1 mM theophylline.	Theophylline	118-130	5'-nucleotidase	Bos taurus	4-19
1535775-0	1992	Soluble low-Km 5"-nucleotidase from electric-ray (Torpedo marmorata) electric organ and bovine cerebral cortex is derived from the glycosyl-phosphatidylinositol-anchored ectoenzyme by phospholipase C cleavage.	Glycosylphosphatidylinositols	131-160	5'-nucleotidase	Bos taurus	15-30
1535775-8	1992	Our results suggest that soluble low-Km 5"-nucleotidase in both electric organ and bovine brain is derived from the membrane-bound GPI-anchored form of the enzyme by the action of a phospholipase C and is not a soluble cytoplasmic enzyme.	Glycosylphosphatidylinositols	131-134	5'-nucleotidase	Bos taurus	40-55
2169262-1	1990	Alkaline phosphatase and 5"-nucleotidase are covalently linked to phosphatidylinositol in bovine fat globule membrane, as demonstrated by their release following treatment with phospholipase C specific for phosphatidylinositol.	Phosphatidylinositols	206-226	5'-nucleotidase	Bos taurus	25-40
23831808-8	2013	An additional interesting aspect of these chromone sulfonamides is their inhibitory activity against ecto-5"-nucleotidase enzyme.	chromone sulfonamides	42-63	5'-nucleotidase	Bos taurus	101-121
2545478-0	1989	Levamisole inhibition of alkaline phosphatase and 5"-nucleotidase of bovine milk fat globule membranes.	Levamisole	0-10	5'-nucleotidase	Bos taurus	50-65
2417294-3	1985	5"-Nucleotidase activity (substrate: 5"-AMP) was 0.25 +/- 0.01 Units/10(6) cells (N = 19) in monolayers and 0.26 +/- 0.01 Units/10(6) cells (N = 20) in homogenates.	Adenosine Monophosphate	37-43	5'-nucleotidase	Bos taurus	0-15
2869783-0	1986	Chemical modification of essential carboxyl group and histidine residue in the plasma-membrane 5"-nucleotidase.	Histidine	54-63	5'-nucleotidase	Bos taurus	95-110
2831062-5	1988	Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate shows two subunits having apparent molecular masses of 65 kDa and 57 kDa respectively, while only one band at 70 kDa is observed in the case of the membrane-bound 5"-nucleotidase.	polyacrylamide	0-14	5'-nucleotidase	Bos taurus	240-255
2831062-5	1988	Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate shows two subunits having apparent molecular masses of 65 kDa and 57 kDa respectively, while only one band at 70 kDa is observed in the case of the membrane-bound 5"-nucleotidase.	Sodium Dodecyl Sulfate	54-76	5'-nucleotidase	Bos taurus	240-255
2831062-14	1988	Finally the exogenous cations, MgCl2 and MnCl2, are necessary for the maximal activity of the cytosolic but not of the membrane 5"-nucleotidase.	Magnesium Chloride	31-36	5'-nucleotidase	Bos taurus	128-143
2831062-14	1988	Finally the exogenous cations, MgCl2 and MnCl2, are necessary for the maximal activity of the cytosolic but not of the membrane 5"-nucleotidase.	manganese chloride	41-46	5'-nucleotidase	Bos taurus	128-143
20501204-1	1988	The kinetic characteristics and the EDTA inhibition of microsomal 5?-nucleotidase from bovine brain cortex were studied and compared with the properties of the enzyme solubilized with Lubrol WX.	Edetic Acid	36-40	5'-nucleotidase	Bos taurus	66-81
6327391-1	1984	To point out the metalloprotein structure of bovine liver plasma membrane 5"-nucleotidase, we studied the inhibition mechanism of the purified enzyme by EDTA: this apparently non-competitive inhibition seems to be dependent on EDTA concentration, pH, temperature and incubation time.	Edetic Acid	153-157	5'-nucleotidase	Bos taurus	74-89
6327391-1	1984	To point out the metalloprotein structure of bovine liver plasma membrane 5"-nucleotidase, we studied the inhibition mechanism of the purified enzyme by EDTA: this apparently non-competitive inhibition seems to be dependent on EDTA concentration, pH, temperature and incubation time.	Edetic Acid	227-231	5'-nucleotidase	Bos taurus	74-89
6321659-0	1984	5"-Nucleotidase from bovine caudate nucleus synaptic plasma membranes: specificity for substrates and cations; study of the carbohydrate moiety by glycosidases.	Carbohydrates	124-136	5'-nucleotidase	Bos taurus	0-15
6321659-3	1984	Effects of metal cations and chelating agents suggest that 5"-nucleotidase is a metalloprotein.	Metals	11-16	5'-nucleotidase	Bos taurus	59-74
6321659-4	1984	Optimal conditions for solubilization of the 5"-nucleotidase were found by using a low concentration of the zwitterionic detergent sulfobetaine 14.	sulfobetaine	131-143	5'-nucleotidase	Bos taurus	45-60
6317380-1	1983	5"-Nucleotidase from bovine liver plasma membranes has been extracted by the zwitterionic detergent sulfobetaine 14, and purified to apparent homogeneity.	sulfobetaine	100-112	5'-nucleotidase	Bos taurus	0-15
6324888-0	1984	Interactions with lectins indicate differences in the carbohydrate composition of the membrane-bound enzymes acetylcholinesterase and 5"-nucleotidase in different cell types.	Carbohydrates	54-66	5'-nucleotidase	Bos taurus	134-149
6300329-3	1983	Although EDTA and 8-hydroxyquinoline inhibit the 5"-nucleotidase from this source, it has not been possible to show the existence of metal ions in the enzyme molecule.	Edetic Acid	9-13	5'-nucleotidase	Bos taurus	49-64
6300329-3	1983	Although EDTA and 8-hydroxyquinoline inhibit the 5"-nucleotidase from this source, it has not been possible to show the existence of metal ions in the enzyme molecule.	Oxyquinoline	18-36	5'-nucleotidase	Bos taurus	49-64
6299197-2	1983	Kinetic studies with a variety of nucleotides and phosphonate analogs show that, although 5"-nucleotidase is a monoesterase like alkaline phosphatase, it more closely resembles 5"-nucleotide phosphodiesterase in its high affinity and specificity for nucleotide binding.	Organophosphonates	50-61	5'-nucleotidase	Bos taurus	90-105
6295180-2	1983	GMP would be broken down to guanosine by the enzyme 5"-nucleotidase on the cytoplasmic (extradiscal) surface of the disks.	guanosine 5'-monophosphorothioate	0-3	5'-nucleotidase	Bos taurus	52-67
6295180-2	1983	GMP would be broken down to guanosine by the enzyme 5"-nucleotidase on the cytoplasmic (extradiscal) surface of the disks.	Guanosine	28-37	5'-nucleotidase	Bos taurus	52-67
6299197-3	1983	5"-Nucleotidase is bound very strongly by an affinity column containing a bound phosphonate analog of ADP but is not bound by an affinity column containing a non nucleotide phosphonate which selectively binds alkaline phosphatase.	Organophosphonates	80-91	5'-nucleotidase	Bos taurus	0-15
6295180-3	1983	The presence of 5"-nucleotidase on the cytoplasmic surface was verified by using sucrose continuous gradients to show its association with the photoreceptors and by using disk preparation and concanavalin A binding to demonstrate its presence on the extradiscal surface.	Sucrose	81-88	5'-nucleotidase	Bos taurus	16-31
6299197-3	1983	5"-Nucleotidase is bound very strongly by an affinity column containing a bound phosphonate analog of ADP but is not bound by an affinity column containing a non nucleotide phosphonate which selectively binds alkaline phosphatase.	Adenosine Diphosphate	102-105	5'-nucleotidase	Bos taurus	0-15
6299197-3	1983	5"-Nucleotidase is bound very strongly by an affinity column containing a bound phosphonate analog of ADP but is not bound by an affinity column containing a non nucleotide phosphonate which selectively binds alkaline phosphatase.	nucleotide phosphonate	162-184	5'-nucleotidase	Bos taurus	0-15
6295180-5	1983	The 5"-nucleotidase on the extradiscal surface is light insensitive, has a broad optimal pH range, shows a divalent cation dependence, and is competitively inhibited by nucleoside di- and triphosphates.	nucleoside di- and triphosphates	169-201	5'-nucleotidase	Bos taurus	4-19
6295180-6	1983	When the data determined experimentally were extrapolated to physiological conditions, we obtained a decay time constant for GMP breakdown by 5"-nucleotidase in the range of 0.4 to 1.06 s. This time constant is in the range of the time constants of the fall of rod cell receptor potential, suggesting a possible role for GMP level in visual transduction.	guanosine 5'-monophosphorothioate	125-128	5'-nucleotidase	Bos taurus	142-157
6295180-6	1983	When the data determined experimentally were extrapolated to physiological conditions, we obtained a decay time constant for GMP breakdown by 5"-nucleotidase in the range of 0.4 to 1.06 s. This time constant is in the range of the time constants of the fall of rod cell receptor potential, suggesting a possible role for GMP level in visual transduction.	guanosine 5'-monophosphorothioate	321-324	5'-nucleotidase	Bos taurus	142-157
6299200-0	1983	5"-deoxy-5"-thioanalogs of adenosine and inosine 5"-monophosphate: studies with 5"-nucleotidase and alkaline phosphatase.	5"-deoxy-5"-thioanalogs	0-23	5'-nucleotidase	Bos taurus	80-95
6299200-6	1983	A(S)MP and I(S)MP were competitive inhibitors of the 5"-nucleotidase hydrolysis of AMP and IMP, respectively, with Ki values of 975 and 13 microM.	Adenosine Monophosphate	83-86	5'-nucleotidase	Bos taurus	53-68
6299200-6	1983	A(S)MP and I(S)MP were competitive inhibitors of the 5"-nucleotidase hydrolysis of AMP and IMP, respectively, with Ki values of 975 and 13 microM.	Inosine Monophosphate	91-94	5'-nucleotidase	Bos taurus	53-68
33979-2	1979	Judging from the recovery of total activity, it is likely that alkaline phosphatase, phosphodiesterase I, and gamma-glutamyl transpeptidase are activated by nonionic detergents, whereas 5"-nucleotidase is somewhat inhibited by the detergents, except for Tween 20, and acid phosphatase is strongly inhibited by all detergents.	Polysorbates	254-262	5'-nucleotidase	Bos taurus	186-201
6248270-2	1980	Both the electrophoretic patterns and substrate specificity of the total 5"-nucleotidase activity at pH 7.4 in serum from 10 normal adults (19-49 years) were identical using various purine and pyrimidine mononucleotides as substrates.	purine	182-188	5'-nucleotidase	Bos taurus	73-88
6248270-2	1980	Both the electrophoretic patterns and substrate specificity of the total 5"-nucleotidase activity at pH 7.4 in serum from 10 normal adults (19-49 years) were identical using various purine and pyrimidine mononucleotides as substrates.	pyrimidine mononucleotides	193-219	5'-nucleotidase	Bos taurus	73-88
6243989-2	1980	5"-Nucleotidase (5"-ribonucleotide phosphohydrolase, EC 3.1.3.5) of bovine milk fat globules can be solubilized by deoxycholate from either isolated globule membranes or washed cream.	Deoxycholic Acid	115-127	5'-nucleotidase	Bos taurus	0-15
141970-8	1977	NaF (10mM) gives a two to three-fold stimulation of enzymatic activity in all fractions studied  The yields of adenylate cyclase, 5"-nucleotidase, and Mg2+-(Na+ +K+)-ATPase are about 6% in the membrane fraction.	Sodium Fluoride	0-3	5'-nucleotidase	Bos taurus	130-145