Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

An antifungal peptide, with a molecular mass of 11 kDa, was isolated from dry seeds of the red lentil (Lens culinaris) using a procedure that involved four chromatographic steps. The antifungal peptide was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and S-Sepharose. The final chromatographic step involved gel filtration by fast protein liquid chromatography on Superdex 75. The antifungal peptide inhibited mycelial growth in Mycosphaerella arachidicola with an IC50 of 36 microM. It also exhibited antifungal activity against Fusarium oxysporum, but there was no inhibitory activity toward tumor cell lines and human immunodeficiency virus type 1 reverse transcriptase (RT).
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PMID:An antifungal peptide from red lentil seeds. 1712 64

A 20-kDa protein with substantial N-terminal sequence homology to thaumatin-like proteins was isolated from ripe fruits of the emperor banana, Musa basjoo cv. 'emperor banana'. The isolation procedure entailed (NH(4))(2)SO(4) precipitation, ion exchange chromatography on DEAE-cellulose, and affinity chromatography on Affi-gel blue gel. The thaumatin-like protein inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola. However, it did not affect the mitogenic response of murine splenocytes or [methyl-(3)H] thymidine incorporation by tumor cells. The activity of HIV-1 reverse transcriptase was slightly inhibited.
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PMID:A thaumatin-like antifungal protein from the emperor banana. 1730 20

We previously found the neuronal cell-type specific promoter and binding partner of the beta isoform of Ca(2+)/calmodulin-dependent protein kinase II (beta CaM kinase II) in rat brain [Donai, H., Morinaga, H., Yamauchi, T., 2001. Genomic organization and neuronal cell type specific promoter activity of beta isoform of Ca(2+)/calmodulin-dependent protein kinase II of rat brain. Mol. Brain Res. 94, 35-47]. In the present study, we purified a protein that binds specifically a promoter region of beta CaM kinase II gene from a nuclear extract of the rat cerebellum using DEAE-cellulose column chromatography, ammonium sulfate fractionation, gel filtration and polyacrylamide gel electrophoresis. The purified protein was identified as rat leucine-rich protein 157 (rLRP157) using tandem mass spectrometry. Then, we prepared its cDNA by reverse transcriptase-polymerase chain reaction (RT-PCR) from poly(A)(+)RNA of rat cerebellum. The rLRP157 cDNA was introduced into mouse neuroblastomaxrat glioma hybrid NG108-15 cells, and cells stably expressing rLRP157 (NG/LRP cells) were isolated. Binding of rLRP157 with the promoter sequence was confirmed by electrophoretic mobility shift assay using nuclear extract of NG/LRP cells. A luciferase reporter gene containing a promoter of beta CaM kinase II was transiently expressed in NG/LRP cells. Under the conditions, the promoter activity was enhanced about 2.6-fold in NG/LRP cells as compared with wild-type cells. The expression of rLRP157 mRNA was paralleled with that of beta CaM kinase II in the adult and embryo rat brain detected by in situ hybridization. Nuclear localization of rLRP157 was confirmed using GFP-rLRP157 fusion protein investigated under a confocal microscope. These results indicate that rLRP157 is one of the proteins binding to, and regulating the activity of, the promoter of beta CaM kinase II.
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PMID:Rat leucine-rich protein binds and activates the promoter of the beta isoform of Ca2+/calmodulin-dependent protein kinase II gene. 1733 62

A trypsin inhibitor, with an N-terminal sequence highly homologous to those of 8-kDa Bowman-Birk trypsin inhibitors, was isolated from the seeds of Hokkaido large black soybeans. The trypsin inhibitor was unadsorbed on SP-Sepharose but adsorbed on DEAE-cellulose and Mono Q. It inhibited proliferation in breast cancer (MCF-7) cells and hepatoma (Hep G2) cells with an IC50 of 35 and 140 microM, respectively. The trypsin inhibitory activity of the inhibitor was completely preserved after exposure to temperatures up to 100 degrees C for 30 min and to the pH range 2-13 for the same duration. The trypsin inhibitor inhibited HIV-1 reverse transcriptase with an IC50 of 38 microM, but was devoid of antifungal activity toward Fusarium oxysporum and Mycosphaerella arachidicola.
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PMID:A Bowman-Birk trypsin inhibitor with antiproliferative activity from Hokkaido large black soybeans. 1788 27

The objective of the present study was to isolate a lectin from fresh fruiting bodies of the mushroom Pleurotus citrinopileatus and examine it for various biological activities. The isolation procedure comprised ion exchange chromatography on DEAE-cellulose, CM-celluloses, and Q-Sepharose, and gel filtration on Superdex 75. A homodimeric 32.4 kDa lectin displaying high hemagglutinating activity was isolated with over 110 fold of purification. Its N-terminal amino acid sequence, QYSQMAQVME, has not been reported for other lectins. The lectin was unadsorbed on DEAE-cellulose in 0.001 M NH4HCO3 buffer (pH 9.4), but adsorbed on CM-cellulose in 0.001 M NH4OAc buffer (pH 4.8) and eluted by approximately 0.05 M NaCl in the same buffer. The lectin was subsequently adsorbed on Q-Sepharose and eluted by a linear gradient of 0-0.2 M NaCl in 10 mM NH4HCO3 buffer (pH 8.5). The lectin was obtained in a purified form after gel filtration by fast protein liquid chromatography on Superdex 75. The hemagglutinating activity of the lectin was inhibited by maltose, O-nitrophenyl-beta-d-galactopyranoside, O/P-nitrophenyl-beta-d-glucuronide and insulin. It was stable at temperatures up to 60 degrees C, and in NaOH and HCl solutions up to 0.1 M and 0.006 M concentration, respectively. It was sensitive to inhibition by HgCl2 and potentiation by AlCl3. The lectin exerted potent antitumor activity in mice bearing sarcoma 180, and caused approximately 80% inhibition of tumor growth when administered intraperitonealy at 5 mg/kg daily for 20 days. It elicited a mitogenic response from murine splenocytes in vitro with the maximal response at a lectin concentration of 2 microM. The lectin inhibited HIV-1 reverse transcriptase with an IC50 of 0.93 microM. It was devoid of antifungal activity.
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PMID:A novel lectin with potent antitumor, mitogenic and HIV-1 reverse transcriptase inhibitory activities from the edible mushroom Pleurotus citrinopileatus. 1796 26

A 17-kDa trypsin inhibitor was isolated from fresh lily bulbs with an isolation procedure that involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose, and gel filtration by FPLC on Superdex 75. Its N-terminal sequence displayed similarity to a short segment of the sequences of the Populus tremula trypsin inhibitor, a putative trypsin inhibitor from Arabidopsis thaliana and sporamin B from sweet potato. The trypsin inhibitor was adsorbed on DEAE-cellulose, unadsorbed on Affi-gel blue gel, and adsorbed on SP-Sepharose. It dose-dependently inhibited trypsin with an IC (50) value of 1.3 microM. There was a stimulatory effect on macrophage production of nitric oxide. Unlike field bean trypsin inhibitor it did not inhibit [methyl-(3)H]thymidine incorporation by leukemia L1210 cells and MBL2 cells when tested up to 100 microM. In contrast to broad bean trypsin inhibitor, there was no inhibitory effect on HIV-1 reverse transcriptase when lily bulb trypsin inhibitor was tested up to 100 microM. The present report is one of the very few on bulbs in contrast to the voluminous literature on seeds.
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PMID:Isolation and characterization of a novel trypsin inhibitor from fresh lily bulbs. 1840 42

Ribosome inactivating proteins (RIPs) are enzymes that inactivate ribosomes by eliminating one or more adenosine residues from rRNA, a 9,567-Da RIP with a novel N-terminal sequence was isolated from fresh fruiting bodies of the mushroom Hypsizigus marmoreus. The protein was unadsorbed on DEAE-cellulose, adsorbed on Affi-gel blue gel, and appeared as a single peak upon gel filtration on Superdex 75. The protein, designated as marmorin, inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF-7 cells, HIV-1 reverse transcriptase activity, and translation in the rabbit reticulocyte lysate system with an IC50 of 0.15 microM, 5 microM, 30 microM, and 0.7 nM, respectively. Compared to RIPs from hairy gourd, bitter gourd, ridge gourd, garden pea, and the mushroom Flammulina velutipes, marmorin was more potent in its antiproliferative activity toward hepatoma (HepG2) and breast cancer (MCF-7) cells, similar in inhibitory potency toward HIV-1 reverse transcriptase (with the exception that it was more potent than ridge gourd RIP and bitter gourd RIP), and less potent in translation-inhibitory potency. Marmorin was devoid of antifungal, protease, RNase, mitogenic, anti-mitogenic, nitric oxide-inducing, hemagglutinating, and trypsin inhibitory activities.
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PMID:Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus. 1875 97

A protein exhibiting an N-terminal amino acid sequence with some similarity to imidazoleglycerol phosphate synthase was purified from fresh Capparis spinosa melon seeds. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, cation exchange chromatography on SP-Sepharose, and finally gel filtration by fast protein liquid chromatography on Superdex 75. The protein was adsorbed using 20 mM Tris-HCl buffer (pH 7.4) and desorbed using 1 M NaCl in the starting buffer from the DEAE-cellulose column and SP-Sepharose column. The protein demonstrated a molecular mass of 38 kDa in gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that it was monomeric. The protein inhibited proliferation of hepatoma HepG2 cells, colon cancer HT29 cells and breast cancer MCF-7 cells with an IC(50) of about 1, 40 and 60 microM, respectively. It inhibited HIV-1 reverse transcriptase with IC(50) of 0.23 microM. It inhibited mycelial growth in the fungus, Valsa mali. It did not exhibit hemagglutinating, ribonuclease, mitogenic or protease inhibitory activities.
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PMID:A protein with antiproliferative, antifungal and HIV-1 reverse transcriptase inhibitory activities from caper (Capparis spinosa) seeds. 1901 43

From the dried fruiting bodies of the toxic mushroom Inocybe umbrinella, a novel lectin with a molecular mass of 17 kDa has been isolated with about 160-fold purification. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, and CM-cellulose, and gel filtration on Superdex 75. Among the carbohydrates tested, raffinose, d-melibiose, alpha-lactose and d(+)-galactose could inhibit the hemagglutinating activity of the lectin. The hemagglutinating activity was stable between 10 and 60 degrees C, in 12.5-100mM HCl, and in 50mM NaOH. The hemagglutinating activity was inhibited by Ca(2+), Mn(2+)and Mg(2+) ions, but was unaffected by Fe(3+), Zn(2+) and Al(3+) ions. The lectin inhibited HIV-1 reverse transcriptase with an IC(50) of 4.7+/-0.2 microM. Proliferation of tumor cells including hepatoma HepG2 cells and breast cancer MCF7 cells was inhibited by the lectin with an IC(50) of 3.5+/-0.2 microM and 7.4+/-0.3 micoM, respectively. The lectin has a unique N-terminal amino acid sequence, DGVLATNAVA. It did not exhibit antifungal activity. The present report is the first on an Inocybe lectin and represents one of the very few reports on lectins from toxic mushrooms.
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PMID:Purification and characterization of a novel lectin from the toxic wild mushroom Inocybe umbrinella. 1911 67

A homodimeric, fructose-binding lectin was isolated from Del Monte bananas by using a protocol that involved ion-exchange chromatography on DEAE-cellulose and SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. Not only fructose, but also glucose, mannose, rhamnose and glucosamine could inhibit the lectin. The N-terminal amino acid sequence of its identical 15-kDa subunits was similar to lectins from other Musa species except for the deletion of the N-terminal glycine residue in Del Monte banana lectin. The hemagglutinating activity was stable up to 80 degrees C and also stable in the range pH 1-13. However, the hemagglutinating activity dwindled to an undetectable level at 90 degrees C. The lectin was capable of eliciting a mitogenic response in murine splenocytes and inducing the expression of the cytokines interferon-gamma, tumor necrosis factor-alpha, and interleukin-2 in splenocytes. The lectin also inhibited proliferation of leukemia (L1210) cells and hepatoma (HepG2) cells and the activity of HIV-1 reverse transcriptase. The additional information obtained in the present study includes demonstration of fructose-binding activity and cytokine-inducing activity of Del Monte banana lectin. Fructose binding is an unusual characteristic of plant lectins. It is possible that the banana lectin can be developed into a useful anti-HIV, immunopotentiating and antitumor agent in view of its trypsin stability and thermostability.
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PMID:Musa acuminata (Del Monte banana) lectin is a fructose-binding lectin with cytokine-inducing activity. 1919 58


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