Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
 31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protein with antifungal and hemagglutinating activities was isolated from dried flageolet beans (Phaseolus vulgaris cv. 'Flageolet Bean'). The protein was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. The protein demonstrated antifungal activity against Mycophaerella arachidicola with an IC50 of 9.8 microM, but was inactive toward Fusarium oxysporum and Botrytis cinerea. Its hemagglutinating activity could not be inhibited by a variety of the sugars tested. The activity was stable up to 60 degrees C. At 70 degrees C, 75% of the hemagglutinating activity remained while no activity was discernible at and above 100 degrees C. The hemagglutinating activity was stable in the presence of a variety of monovalent, divalent and trivalent chlorides, and also when the ambient pH changed from 3 to 12. It did not exert any mitogenic activity on mouse splenocytes in vitro. Neither did it inhibit HIV-1 reverse transcriptase. It inhibited [3H-methyl]-thymidine incorporation into leukemia L1210 cells with an IC50 of about 4 microM.
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PMID:An antifungal protein from flageolet beans. 1602 1

A homodimeric lactose-binding lectin with a molecular mass of 64kDa was isolated from fresh fruiting bodies of the split gill mushroom Schizophyllum commune. The N-terminal sequence of the lectin is similar to a part of the sequence of the cell division protein from Gleobacter violaceus. The lectin was isolated by using a procedure which involved ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 40 degrees C, and in concentrations of NaOH and HCl solution up to 125 and 25mM, respectively. The lectin exhibited potent mitogenic activity toward mouse splenocytes, antiproliferative activity toward tumor cell lines, and inhibitory activity toward HIV-1 reverse transcriptase. It was devoid of antifungal activity.
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PMID:A novel homodimeric lactose-binding lectin from the edible split gill medicinal mushroom Schizophyllum commune. 1614 99

A chromatographic procedure consisting of ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose, and gel filtration by fast performance liquid chromatography on Supedex 75 was utilized to isolate a 10 kDa antifungal peptide from coconut flesh. The peptide was unadsorbed on DEAE-cellulose, but adsorbed on Affi-gel blue gel and CM-cellulose. It displayed antifungal activity against Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola. The IC50 values of its inhibitory activities on mycelial growth in M. arachidicola and HIV-1 reverse transcriptase activity were respectively 1.2 and 52.5 microM.
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PMID:An antifungal peptide from the coconut. 1630 82

A protein, with a novel N-terminal amino acid sequence and a molecular mass of 30 kDa, was purified from fresh Smilax glabra rhizomes by adsorption on DEAE-cellulose, CM-cellulose, Con A-Sepharose, and Mono S, and by fast protein liquid chromatography-gel filtration on Superdex 75. The protein, designated as smilaxin, stimulated uptake of [methyl-3H]thymidine by murine splenocytes, peritoneal macrophages, and bone marrow cells, and production of nitric oxide by peritoneal macrophages. It inhibited uptake of [methyl-3H]thymidine by MBL2 and PU5 tumor cells but not uptake by S180 and L1210 cells. Smilaxin augmented glucose uptake into rat adipose tissue. It attenuated the activity of HIV-1-reverse transcriptase with an IC50 of 5.6 microM. However, it did not display hemagglutinating, antifungal or translation-inhibitory activities, indicating that it is not a lectin, an antifungal protein, or a ribosome-inactivating protein.
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PMID:Smilaxin, a novel protein with immunostimulatory, antiproliferative, and HIV-1-reverse transcriptase inhibitory activities from fresh Smilax glabra rhizomes. 1637 60

An antifungal protein with a molecular mass of 11 kDa and a lysine-rich N-terminal sequence was isolated from the seeds of the pea Pisum sativum var. arvense Poir. The antifungal protein was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. It exerted antifungal activity against Physalospora piricola with an IC50 of 0.62 microM, and also antifungal activity against Fusarium oxysporum and Mycosphaerella arachidicola. It inhibited human immunodeficiency virus type 1 reverse transcriptase with an IC50 of 4.7 microM.
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PMID:An antifungal protein from the pea Pisum sativum var. arvense Poir. 1657 76

A protein demonstrating laccase activity and potent inhibitory activity towards human immunodeficiency virus (HIV)-1 reverse transcriptase (IC50 1.2 microM) was isolated from fresh fruiting bodies of the medicinal mushroom Ganoderma lucidum. The laccase had a novel N-terminal sequence and a molecular mass of 75 kDa, which is higher than the range (55-56 kDa) reported for most other mushroom laccases. It was isolated by sequential chromatography on DEAE-cellulose and Affi-gel blue gel and adsorption on Con A-Sepharose. Unlike some of the previously isolated laccases, it was adsorbed only on Con A-Sepharose. The enzyme required a pH of 3-5 and a temperature of 70 degrees C to exhibit maximal activity. Minimal activity was detected at pH 6 and 7. Activity was undetectable at pH 8 and 9 and after exposure to 100 degrees C for 10 min.
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PMID:A laccase from the medicinal mushroom Ganoderma lucidum. 1663 32

A lectin, with a molecular mass of 79 kDa, and with specificity toward rhamnose and O-nitrophenyl-beta-D-galactopyranoside, was isolated from samta tomato fruits. The procedure entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose and gel filtration by fast protein liquid chromatography on Superdex 75. The lectin was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. The lectin was stable up to 70 degrees C. The lectin activity was potentiated by NaOH solutions (25-100 mM), but was reduced by 50 and 100 mM HCl solutions. The activity of the lectin was reduced in the presence of CaCl(2), MgCl(2) and ZnCl(2), but was potentiated by 5 and 10 mM AlCl(3) solutions. The lectin stimulated the mitogenic response in mouse splenocytes and inhibited human immunodeficiency virus-1 reverse transcriptase with an IC(50) of 6.2 microM.
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PMID:A lectin with some unique characteristics from the samta tomato. 1677 25

The aqueous extracts and ethanol precipitates of aqueous extracts of 18 medicinal herbs traditionally used in China were screened for their ability to inhibit human immunodeficiency virus type-1 reverse transcriptase (HIV-1 RT) in-vitro. Among the samples screened at a concentration of 500 microg mL-1, dried rose (Rosa rugosa) flowers showed the strongest inhibition. The ethanol precipitate of the aqueous extract of R. rugosa was processed and two components (P1 and P2) were obtained after ion exchange chromatography on DEAE-cellulose. Then, P1-a (Mr 150 kDa) and P1-b (Mr 8 kDa) were isolated from P1 by gel filtration on Sephadex G-200. They inhibited the activity of HIV-1 RT with an IC50 of 158 nM and 148.16 microg mL-1 (18.5 microM), respectively. Further structural analyses revealed that P1-a was a polysaccharide-peptide complex, and P1-b was a polymer consisting of acteoside and acteoside derivatives identified by Fourier transform infrared spectroscopy, nuclear magnetic resonance, assays of carbohydrate and protein contents and high-performance liquid chromatography electrospray ionization mass spectrometry.
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PMID:Compounds from rose (Rosa rugosa) flowers with human immunodeficiency virus type 1 reverse transcriptase inhibitory activity. 1694 87

A 67-kDa hemagglutinin composed of two identical subunits was purified from Phaseolus vulgaris cv. 'Dark Red Kidney Bean'. It was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel. The hemagglutinin was highly purified after the two aforementioned chromatographic steps as revealed by a single peak in gel filtration on Superdex 75 and a single band in SDS-PAGE. The hemagglutinating activity was stable between 25 degrees C and 70 degrees C, and between pH 4 and pH 11, and in the presence of a variety of divalent metal chlorides at 500 mM concentration. The activity was reduced by 50% at 80 degrees C, and also when the pH was lowered to 3 or elevated to 12. The activity was reduced by 75% in the presence of 250 mM KCl or NaCl. A variety of sugars tested failed to inhibit the hemagglutinating activity of the hemagglutinin. Although the hemagglutinin exhibited mitogenic activity toward murine splenocytes, it had no effect on the activity of HIV-1 reverse transcriptase or mycelial growth in the fungi Botrytis cinerea, Fusarium oxysporum and Mycosphaerella arachidicola. It exerted an antiproliferative activity on leukemia L1210 cells.
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PMID:A hemagglutinin with mitogenic activity from dark red kidney beans. 1694 95

Hot water extracts of 16 species of mushrooms, including both edible and medicinal mushrooms, were screened for human immunodeficiency virus (HIV)-1 reverse transcriptase (RT) inhibitory activity. Extracts of Lactarius camphoratus, Trametes suaveolens, Sparassis crispa, Pleurotus sajor-caju, Pleurotus pulmonarius, and Russula paludosa elicited over 50% inhibition when tested at the concentration of 1 mg/ml. The extract of R. paludosa demonstrated the highest inhibitory activity on HIV-1 RT (97.6%). Fraction SU2, purified from R. paludosa extract by anion exchange chromatography on DEAE-cellulose and gel filtration on Superdex 75, exhibited potent inhibitory activity on HIV-1 RT. At the concentrations of 1 mg/ml, 0.2 mg/ml, and 0.04 mg/ml, the inhibition ratios were 99.2%, 89.3%, and 41.8%, respectively, giving an IC50 of 11 microM. The molecular mass of SU2 was 4.5 kDa and its N-terminal amino acid sequence was determined to be KREHGQHCEF. The peptide was devoid of hemagglutinating, ribonuclease, antifungal, protease, protease inhibitory, and laccase activities.
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PMID:A peptide with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Russula paludosa. 1711 95


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