PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 32093479-3 2020 Here, sum frequency generation (SFG) vibrational spectroscopy and laser scanning confocal microscopy (LSCM) were applied to study the interaction between honey bee venom phospholipase A2 (bvPLA2) and the negatively charged DPPG bilayer. 1,2-dipalmitoylphosphatidylglycerol 223-227 phospholipase A2 Apis mellifera 170-186 33443641-2 2021 RESULTS: The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee (Apis mellifera lamarckii) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE-cellulose and Sephacryl S-300 columns. DEAE-Cellulose 199-213 phospholipase A2 Apis mellifera 13-29 33443641-2 2021 RESULTS: The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee (Apis mellifera lamarckii) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE-cellulose and Sephacryl S-300 columns. DEAE-Cellulose 199-213 phospholipase A2 Apis mellifera 31-35 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. cupric ion 71-75 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Nickel(2+) 77-81 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. ammonium ferrous sulfate 83-87 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Carbon Dioxide 99-103 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Zinc 156-160 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Manganese(2+) 162-166 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Sodium Azide 168-172 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Phenylmethylsulfonyl Fluoride 174-178 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. N-methylmaleimide 180-197 phospholipase A2 Apis mellifera 34-38 33443641-4 2021 The optimal activity of bee venom PLA2 was attained at pH 8 and 45 C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Edetic Acid 203-207 phospholipase A2 Apis mellifera 34-38 32502555-1 2020 Many organisms, ranging from plants to mammals, contain phospholipase A2 enzymes (PLA2s), which catalyze the production of lysophospholipids and fatty acid proinflammatory mediators. Lysophospholipids 123-140 phospholipase A2 Apis mellifera 56-72 32502555-1 2020 Many organisms, ranging from plants to mammals, contain phospholipase A2 enzymes (PLA2s), which catalyze the production of lysophospholipids and fatty acid proinflammatory mediators. Fatty Acids 145-155 phospholipase A2 Apis mellifera 56-72 32093479-3 2020 Here, sum frequency generation (SFG) vibrational spectroscopy and laser scanning confocal microscopy (LSCM) were applied to study the interaction between honey bee venom phospholipase A2 (bvPLA2) and the negatively charged DPPG bilayer. 1,2-dipalmitoylphosphatidylglycerol 223-227 phospholipase A2 Apis mellifera 188-194 31679116-0 2020 The anticoagulant effect of Apis mellifera phospholipase A2 is inhibited by CORM-2 via a carbon monoxide-independent mechanism. Carbon Monoxide 89-104 phospholipase A2 Apis mellifera 43-59 31679116-2 2020 Ruthenium (Ru)-based carbon monoxide releasing molecules (CORM) inhibit snake venoms that are anticoagulant and contain PLA2. Ruthenium 0-14 phospholipase A2 Apis mellifera 120-124 31679116-2 2020 Ruthenium (Ru)-based carbon monoxide releasing molecules (CORM) inhibit snake venoms that are anticoagulant and contain PLA2. Carbon Monoxide 21-36 phospholipase A2 Apis mellifera 120-124 31679116-4 2020 This study sought to identify anticoagulant properties of bee venom PLA2 via catalysis of plasma phospholipids required for thrombin generation. Phospholipids 97-110 phospholipase A2 Apis mellifera 68-72 31679116-5 2020 Another goal was to determine if Ru-based CORM inhibit bee venom PLA2 via carbon monoxide release or via potential binding of reactive Ru species to a key histidine residue in the catalytic site of the enzyme. Ruthenium 33-35 phospholipase A2 Apis mellifera 65-69 20443212-1 2010 Bee venom phospholipase A(2) (BvPLA(2)) is a lipolytic enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerophospholipids to liberate free fatty acids and lysophospholipids. Glycerophospholipids 117-137 phospholipase A2 Apis mellifera 30-38 29149234-0 2017 Calcium-dependent hydrolysis of supported planar lipids was triggered by honey bee venom phospholipase A2 with the right orientation at the interface. Calcium 0-7 phospholipase A2 Apis mellifera 89-105 29149234-1 2017 Hydrolysis of planar phospholipids catalyzed by honey bee venom phospholipase A2 (bvPLA2) was studied. Phospholipids 21-34 phospholipase A2 Apis mellifera 64-80 29149234-1 2017 Hydrolysis of planar phospholipids catalyzed by honey bee venom phospholipase A2 (bvPLA2) was studied. Phospholipids 21-34 phospholipase A2 Apis mellifera 82-88 23474269-10 2013 Suramin markedly inhibited the PLA2 activity in a concentration-dependent way (1-30 muM). Suramin 0-7 phospholipase A2 Apis mellifera 31-35 20443212-1 2010 Bee venom phospholipase A(2) (BvPLA(2)) is a lipolytic enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerophospholipids to liberate free fatty acids and lysophospholipids. Fatty Acids, Nonesterified 150-166 phospholipase A2 Apis mellifera 30-38 20443212-1 2010 Bee venom phospholipase A(2) (BvPLA(2)) is a lipolytic enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerophospholipids to liberate free fatty acids and lysophospholipids. Lysophospholipids 171-188 phospholipase A2 Apis mellifera 30-38 19463845-11 2009 In isolated kidney, the PLA(2) from B. caissarum increased the perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate, and sodium, potassium and chloride levels of excretion. Sodium 156-162 phospholipase A2 Apis mellifera 24-29 19539776-7 2009 Comparative analysis revealed that the mature Bi-PLA(2) (136 amino acids) possesses features consistent with other bee PLA(2)s, including ten conserved cysteine residues, as well as a highly conserved Ca(2+)-binding site and active site. Cysteine 152-160 phospholipase A2 Apis mellifera 49-55 19539776-9 2009 The mature Bi-PLA(2) purified from the venom of B. ignitus worker bees hydrolyzed DBPC, a known substrate of PLA(2). Butylated Hydroxytoluene 82-86 phospholipase A2 Apis mellifera 14-20 19539776-9 2009 The mature Bi-PLA(2) purified from the venom of B. ignitus worker bees hydrolyzed DBPC, a known substrate of PLA(2). Butylated Hydroxytoluene 82-86 phospholipase A2 Apis mellifera 109-115 19463845-11 2009 In isolated kidney, the PLA(2) from B. caissarum increased the perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate, and sodium, potassium and chloride levels of excretion. Potassium 164-173 phospholipase A2 Apis mellifera 24-29 19463845-11 2009 In isolated kidney, the PLA(2) from B. caissarum increased the perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate, and sodium, potassium and chloride levels of excretion. Chlorides 178-186 phospholipase A2 Apis mellifera 24-29 19463845-13 2009 In conclusion, PLA(2), a group III phospholipase isolated from the sea anemone B. caissarum, exerted effects on renal function and induced insulin secretion in conditions of high glucose concentration. Glucose 179-186 phospholipase A2 Apis mellifera 15-20 11824812-0 2002 Analysis of N-glycosylation of phospholipase A2 from venom of individual bees by microbore high-performance liquid chromatography-electrospray mass spectrometry using an ion trap mass spectrometer. Nitrogen 12-13 phospholipase A2 Apis mellifera 31-47 19714242-5 2009 The analysis of approximately 4000 pseudopodia reveals that step and turn pseudopodia are drawn from a probability distribution that is determined by cGMP/PLA2 signaling pathways. Cyclic GMP 150-154 phospholipase A2 Apis mellifera 155-159 17165844-3 2006 Using this method, isobaric N-glycans released from honey bee phospholipase A2 and Arabidopsis thaliana glycoproteins were separated by normal-phase chromatography and subsequently identified by key fragment ions in the MALDI-TOF/TOF tandem mass spectra. n-glycans 28-37 phospholipase A2 Apis mellifera 62-78 11824812-1 2002 The N-linked oligosaccharides were released from the phospholipase A2 (PLA) with glycopeptidases and reductively aminated with the chromophore, p-aminobenzoic acid ethyl ester (ABEE). n-linked oligosaccharides 4-29 phospholipase A2 Apis mellifera 53-69 11824812-1 2002 The N-linked oligosaccharides were released from the phospholipase A2 (PLA) with glycopeptidases and reductively aminated with the chromophore, p-aminobenzoic acid ethyl ester (ABEE). n-linked oligosaccharides 4-29 phospholipase A2 Apis mellifera 71-74 11824812-1 2002 The N-linked oligosaccharides were released from the phospholipase A2 (PLA) with glycopeptidases and reductively aminated with the chromophore, p-aminobenzoic acid ethyl ester (ABEE). Benzocaine 144-175 phospholipase A2 Apis mellifera 53-69 11824812-1 2002 The N-linked oligosaccharides were released from the phospholipase A2 (PLA) with glycopeptidases and reductively aminated with the chromophore, p-aminobenzoic acid ethyl ester (ABEE). Benzocaine 144-175 phospholipase A2 Apis mellifera 71-74 11754875-4 2002 Heparin (10-300 U/mL) concentration-dependently inhibited the neutrophil migration induced by piratoxin-I, bothropstoxin-II, and N. m. mocambique and A. mellifera venom PLA2s (100 microg/mL each), but failed to affect the migration induced by porcine pancreas PLA2. Heparin 0-7 phospholipase A2 Apis mellifera 169-173 10485384-3 1999 In this study, we investigated the involvement of N-glycan on phospholipase A2 (PLA2), the major allergen of honeybee venom, in in vivo synthesis of specific IgE in mice. n-glycan 50-58 phospholipase A2 Apis mellifera 62-78 10758272-2 2000 By using gel filtration on Sephadex G-100, followed by high performance reversed phase chromatography in a C-18 column under acetonitrile/water gradient, the agelotoxin was purified: a toxin presenting phospholipase A(2) (PLA(2)) activity, which occurs under equilibrium of three different aggregation states: monomer (mol. agelotoxin 158-168 phospholipase A2 Apis mellifera 222-228 10758272-8 2000 The PLA(2) catalytic activity of agelotoxin changes according to its state of aggregation (from 833 to 12533 micromol mg(-1) min(-1)) and both the monomeric and oligomeric forms present lowest activities than the PLA(2) from Apis mellifera venom and hornetin from Vespa basalis. agelotoxin 33-43 phospholipase A2 Apis mellifera 4-10 10758272-8 2000 The PLA(2) catalytic activity of agelotoxin changes according to its state of aggregation (from 833 to 12533 micromol mg(-1) min(-1)) and both the monomeric and oligomeric forms present lowest activities than the PLA(2) from Apis mellifera venom and hornetin from Vespa basalis. agelotoxin 33-43 phospholipase A2 Apis mellifera 213-219 10758272-9 2000 Agelotoxin is also a very potent direct hemolysin; the monomer of agelotoxin presented hemolytic actions until 200 times higher than the PbTx from P. paulista, 740 times higher than the PLA(2) from A. mellifera, 570 times higher than that of neutral PLA(2) from N. nigricolis and about 1250 times than that of cardiotoxin from Naja naja atra venom. agelotoxin 0-10 phospholipase A2 Apis mellifera 186-192 10758272-9 2000 Agelotoxin is also a very potent direct hemolysin; the monomer of agelotoxin presented hemolytic actions until 200 times higher than the PbTx from P. paulista, 740 times higher than the PLA(2) from A. mellifera, 570 times higher than that of neutral PLA(2) from N. nigricolis and about 1250 times than that of cardiotoxin from Naja naja atra venom. agelotoxin 0-10 phospholipase A2 Apis mellifera 250-256 10758272-9 2000 Agelotoxin is also a very potent direct hemolysin; the monomer of agelotoxin presented hemolytic actions until 200 times higher than the PbTx from P. paulista, 740 times higher than the PLA(2) from A. mellifera, 570 times higher than that of neutral PLA(2) from N. nigricolis and about 1250 times than that of cardiotoxin from Naja naja atra venom. agelotoxin 66-76 phospholipase A2 Apis mellifera 250-256 10665801-11 2000 Since heparin reduced paw oedema induced by PLA2 from Naja mocambique mocambique venom it is likely that this sPLA2 is similar to the novel heparin-sensitive PLA2 found in mast cells. Heparin 6-13 phospholipase A2 Apis mellifera 44-48 10665801-11 2000 Since heparin reduced paw oedema induced by PLA2 from Naja mocambique mocambique venom it is likely that this sPLA2 is similar to the novel heparin-sensitive PLA2 found in mast cells. Heparin 6-13 phospholipase A2 Apis mellifera 111-115 11085411-7 2000 The analysis of phospholipase A2 from the venom of individual bees indicated that the variation and relative abundances of different glycopeptides were similar between the younger and the older bees. Glycopeptides 133-146 phospholipase A2 Apis mellifera 16-32 10485384-3 1999 In this study, we investigated the involvement of N-glycan on phospholipase A2 (PLA2), the major allergen of honeybee venom, in in vivo synthesis of specific IgE in mice. n-glycan 50-58 phospholipase A2 Apis mellifera 80-84 9990137-1 1999 A phospholipase A2 (PLA2) inhibitor was purified from the blood plasma of a sea krait, Laticauda semifasciata, by sequential chromatography on Sephadex G-200, Mono Q, and Phenyl Sepharose columns. sephadex 143-157 phospholipase A2 Apis mellifera 20-24 9990137-1 1999 A phospholipase A2 (PLA2) inhibitor was purified from the blood plasma of a sea krait, Laticauda semifasciata, by sequential chromatography on Sephadex G-200, Mono Q, and Phenyl Sepharose columns. phenyl-sepharose 171-187 phospholipase A2 Apis mellifera 20-24 9604292-6 1998 The catalytic activities of polybitoxins (from 18 to 771 mumoles/mg per minute) are lower than that of PLA2 from Apis mellifera venom and hornetin from Vespa basalis. polybitoxins 28-40 phospholipase A2 Apis mellifera 103-107 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxins 11-23 phospholipase A2 Apis mellifera 278-282 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxins 11-23 phospholipase A2 Apis mellifera 339-343 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxins 75-87 phospholipase A2 Apis mellifera 278-282 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxins 75-87 phospholipase A2 Apis mellifera 339-343 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxin 11-22 phospholipase A2 Apis mellifera 278-282 9604292-8 1998 All of the polybitoxins were very potent direct hemolysins, especially the polybitoxins-III and IV, which are as potent as the lethal toxin from V. basalis and hornetin from Vespa flavitarsus, respectively; polybitoxin-IV presented hemolytic action 20 times higher than that of PLA2 from A. meliferra, 17 times higher than that of neutral PLA2 from Naja nigricolis and about 37 times higher than that of cardiotoxin from Naja naja atra venom. polybitoxin 11-22 phospholipase A2 Apis mellifera 339-343 1376112-0 1992 The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. Carbohydrates 24-36 phospholipase A2 Apis mellifera 104-120 8504812-0 1993 Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2. Nitrogen 26-27 phospholipase A2 Apis mellifera 75-91 8504812-0 1993 Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2. linked carbohydrate 28-47 phospholipase A2 Apis mellifera 75-91 8504812-5 1993 Four compounds, which comprised 10% of the oligosaccharide pool from phospholipase A2, contained a rarely found terminal element with N-acetylgalactosamine. Oligosaccharides 43-58 phospholipase A2 Apis mellifera 69-85 8504812-6 1993 The structures of the 14 N-glycans from honeybee phospholipase A2 can be arranged into the following three series: [formula: see text] n-glycans 25-34 phospholipase A2 Apis mellifera 49-65 1344712-0 1992 Alpha 1-6(alpha 1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase A2. Asparagine 43-53 phospholipase A2 Apis mellifera 98-114 1344712-0 1992 Alpha 1-6(alpha 1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase A2. Acetylglucosamine 60-79 phospholipase A2 Apis mellifera 98-114 9115249-13 1997 On the other hand, treatment of IpTxi with p-bromophenacylbromide, a specific inhibitor of PLA2 activity, greatly reduced the capacity of IpTxi to inhibit RyRs. 4-bromophenacyl bromide 43-65 phospholipase A2 Apis mellifera 91-95 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. [3h]arachidonate 81-97 phospholipase A2 Apis mellifera 10-26 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. [3h]arachidonate 81-97 phospholipase A2 Apis mellifera 28-32 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. [3h]diacylglycerol 102-120 phospholipase A2 Apis mellifera 10-26 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. [3h]diacylglycerol 102-120 phospholipase A2 Apis mellifera 28-32 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. N-acylethanolamines 157-160 phospholipase A2 Apis mellifera 10-26 8906547-6 1996 Exogenous phospholipase A2 (PLA2) (Apis mellifera) and PLC (B. cereus) mobilized [3H]arachidonate and [3H]diacylglycerol, respectively, but had no effect on NAE formation under these conditions. N-acylethanolamines 157-160 phospholipase A2 Apis mellifera 28-32 7676467-0 1995 Arthropod venom citrate inhibits phospholipase A2. Citric Acid 16-23 phospholipase A2 Apis mellifera 33-49 1450215-1 1992 Bee venom phospholipase A2 (BV-PLA2) is a hydrolytic enzyme that specifically cleaves the sn-2 acyl bond of phospholipids at the lipid/water interface. Phospholipids 108-121 phospholipase A2 Apis mellifera 10-26 1450215-1 1992 Bee venom phospholipase A2 (BV-PLA2) is a hydrolytic enzyme that specifically cleaves the sn-2 acyl bond of phospholipids at the lipid/water interface. Water 135-140 phospholipase A2 Apis mellifera 10-26 1376112-3 1992 The interaction of anti-(horseradish peroxidase) antiserum with PLA2 suggests the existence of a carbohydrate determinant common to both glycoproteins. Carbohydrates 97-109 phospholipase A2 Apis mellifera 64-68 34972703-6 2022 In vitro, DEA inhibited hemolysis caused by the brown recluse spider venom and rPLD and suppressed phospholipase A2 activity in a dose-dependent manner. diethyl azelate 10-13 phospholipase A2 Apis mellifera 99-115 3103628-3 1987 Phospholipase A2 isolated from bee venom (Apis mellifera) was the most sensitive to inactivation by manoalide (IC50 approximately equal to 0.12 microM). manoalide 100-109 phospholipase A2 Apis mellifera 0-16 6441310-7 1984 Indomethacin and EDTA completely abolished both phospholipase A2 induced platelet shape change and aggregation, while mepacrine, prostaglandin E1, verapamil and nitroprusside inhibited only the aggregation response. Indomethacin 0-12 phospholipase A2 Apis mellifera 48-64 6441310-7 1984 Indomethacin and EDTA completely abolished both phospholipase A2 induced platelet shape change and aggregation, while mepacrine, prostaglandin E1, verapamil and nitroprusside inhibited only the aggregation response. Edetic Acid 17-21 phospholipase A2 Apis mellifera 48-64 6441310-9 1984 Phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol inhibited the phospholipase A2-induced platelet aggregation. Phosphatidylcholines 0-19 phospholipase A2 Apis mellifera 85-101 6441310-9 1984 Phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol inhibited the phospholipase A2-induced platelet aggregation. phosphatidylethanolamine 21-45 phospholipase A2 Apis mellifera 85-101 6441310-9 1984 Phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol inhibited the phospholipase A2-induced platelet aggregation. Phosphatidylinositols 50-70 phospholipase A2 Apis mellifera 85-101 6441310-11 1984 Pre-treatment of platelet suspension with phospholipase A2 from N. n. atra or A. mellifera venom (50 micrograms/ml) inhibited platelet aggregation induced by sodium arachidonate or collagen, but not that induced by thrombin or ionophore A-23187. Arachidonic Acid 158-177 phospholipase A2 Apis mellifera 42-58 6658811-2 1983 The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Carbohydrates 117-129 phospholipase A2 Apis mellifera 76-92 2444130-0 1987 Specific interaction of IgE antibodies with a carbohydrate epitope of honey bee venom phospholipase A2. Carbohydrates 46-58 phospholipase A2 Apis mellifera 86-102 3956155-0 1986 Characteristics of the asparagine-linked oligosaccharide from honey-bee venom phospholipase A2. asparagine-linked oligosaccharide 23-56 phospholipase A2 Apis mellifera 78-94 7131592-0 1982 Effect of phospholipase A2 on calcium transport in brain synaptosomes. Calcium 30-37 phospholipase A2 Apis mellifera 10-26 7131592-2 1982 Phospholipase A2 initially caused an increase of synaptosome respiration and subsequently inhibited their oxygen uptake, but this effect was completely abolished in BSA-containing media. Oxygen 106-112 phospholipase A2 Apis mellifera 0-16 7131592-5 1982 However, depolarization-dependent release of [3H]GABA from synaptosomes treated with phospholipase A2 was significantly inhibited. Tritium 45-48 phospholipase A2 Apis mellifera 85-101 7131592-5 1982 However, depolarization-dependent release of [3H]GABA from synaptosomes treated with phospholipase A2 was significantly inhibited. gamma-Aminobutyric Acid 49-53 phospholipase A2 Apis mellifera 85-101 7131592-6 1982 We suggest that the inhibition of depolarization-dependent influx of 45Ca into synaptosomes treated with phospholipase A2 may be attributed to the lesion of the specific function of plasma membrane rather than to the impairment of the calcium-sequestrating function of intraterminal structures. Calcium 235-242 phospholipase A2 Apis mellifera 105-121 7295818-1 1981 The effect of purified phospholipase A2 from venom of the bee Apis mellifica and from venom of the cobra Naja naja oxiana on the Na+-dependent high affinity choline transport into the synaptosomes of rabbit corpus striatum (active uptake) was studied. Choline 157-164 phospholipase A2 Apis mellifera 23-39