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)

Phospholipase A2 (PLA2) activity was investigated in various tissues of male and female red sea bream. In both male and female fishes, the specific activity of PLA2 in the gills was 70 times higher than that in other tissues, such as the adipose tissue, intestine, and hepatopancreas. Therefore, we tried to purify PLA2 from the gill filaments of red sea bream to near homogeneity by sequential chromatography on Q-Sepharose Fast Flow, Butyl-Cellulofine, and DEAE-Sepharose Fast Flow columns, and by reversed-phase high-performance liquid chromatography. Two minor and one major PLA2, tentatively named G-1, G-2 and G-3 PLA2, were purified, and all showed a single band with an apparent molecular mass of approximately 15 kDa by sodium dodecylsulfate-polyacrylamide gel electrophoresis. The exact molecular mass values of G-1, G-2, and G-3 PLA2 were 14,040, 14,040 and 14,005 Da, respectively. G-1, G-2, and G-3 PLA2 had a Cys 11 and were all identical in N-terminal amino acid sequences from Ala-1 to Glu-56. A full-length cDNA encoding G-3 PLA2 was cloned by reverse transcriptase-polymerase chain reaction and rapid amplification of cDNA ends methods, and G-3 PLA2 was found to be classified to group IB PLA2 from the deduced amino acid sequence. G-1, G-2, and G-3 PLA2 had a pH optimum in an alkaline region at around pH 9-10 and required Ca2+ essentially for enzyme activity, using a mixed-micellar phosphatidylcholine substrate with sodium cholate. These results demonstrate that three group I PLA2, G-1, G-2, and G-3 PLA2, are expressed in the gill filaments of red sea bream.
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PMID:Purification, characterization, and molecular cloning of group I phospholipases A2 from the gills of the red sea bream, Pagrus major. 1120 98

From the roots of the Chinese ginseng Panax ginseng a protein designated panaxagin with ribonuclease activity, but possessing a sequence distinct from ribonucleases previously reported from ginseng calluses, was isolated. The purification protocol employed comprised extraction with cold saline, (NH4)2SO4 precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose, and gel filtration on Superdex 75 by fast protein liquid chromatography. The purified protein was composed of two identical subunits each with a molecular weight of 26 kDa. Its N-terminal amino acid sequence exhibits sites of similarity with the sequences of plant ribosome inactivating proteins and fungal ribonucleases. The spectrum of biological activities of panaxagin encompassed ribonuclease activity toward yeast transfer RNA, translation-inhibitory activity in a rabbit reticulocyte lysate system, and antifungal activity against fungi including Coprinus comatus and Fusarium oxysporum, but not against Rhizoctonia solani. In addition it displayed an inhibitory activity against human immunodeficiency virus reverse transcriptase and succinylation augmented this activity.
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PMID:Panaxagin, a new protein from Chinese ginseng possesses anti-fungal, anti-viral, translation-inhibiting and ribonuclease activities. 1120 66

From the fruiting bodies of the edible mushroom Flammulina velutipes a single-chained ribosome inactivating protein with a molecular weight of 13.8 kDa was isolated with a procedure involving ion exchange chromatography on DEAE-cellulose and SP-Sepharose and affinity chromatography on Affi-gel blue gel. The protein was novel in that it possessed a molecular weight lower than those of previously reported RIPs and that it was capable of inhibiting human immunodeficiency virus (HIV-1) reverse transcriptase, beta-glucosidase and beta-glucuronidase. Its N-terminal sequence exhibited a certain degree of similarity to those of plant ribosome inactivating proteins.
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PMID:Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies. 1132 20

From the roots of the Chinese medicinal herb Pseudostellaria heterophylla a single-chained lectin with a molecular weight of 36 kDa and high hemagglutinating activity was isolated. The lectin was adsorbed on DEAE-cellulose in 10 mM Tris-HCI buffer (pH 7.4) and was eluted by the same buffer containing 50 mM NaCl. It was adsorbed on SP-Sepharose in 10mM NH4OAc (pH 4.5) and eluted by approximately 0.5 M NaCl in the same buffer. The hemagglutinating activity of the lectin could not be inhibited by a large variety of monosaccharides, but was largely abrogated by exposure to 0.05 M HCl, 0.05M NaOH or 80 degrees C. However, about 50% of the activity remained after exposure to 0.025M NaOH or 40 degrees C. Despite possession of an N-terminal sequence exhibiting some similarity to thaumatin-like proteins with antifungal activity, the lectin was devoid of antifungal activity. The lectin exerted some inhibitory effect on the glycohydrolases alpha-glucosidase, beta-glucosidase and beta-glucuronidase which are involved in HIV infection but had no suppressive action on human immunodeficiency virus-type 1 reverse transcriptase.
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PMID:A novel lectin from Pseudostellaria heterophylla roots with sequence simularity to Kunitz-type soybean trypsin inhibitor. 1144 23

A novel antifungal protein, designated chrysancorin, was isolated from seeds of Chrysanthemum coronarium var. spatiosum with a procedure involving ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue resin, ion exchange chromatography on SP-Sepharose and FPLC-gel filtration on Superdex 75. The N-terminus of chrysancorin displays sequence similarity to the genomic sequence of chromosome 1 from Arabidopsis thaliana BAC T19E23. Chrysancorin exhibits a molecular mass of 13.4 kDa in gel filtration and SDS-polyacrylamide gel electrophoresis. It stimulates the proliferation of mouse splenocytes and inhibits the activity of human immunodeficiency virus-1 reverse transcriptase. The protein possesses antifungal activity against Botrytis cinerea, Mycosphaerella arachidicola and Physalospora piricola, but not against Rhizoctonia solani, Fusarium oxysporum and Coprinus comatus. However, we could not detect antibacterial activity against a variety of bacteria.
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PMID:Purification of chrysancorin, a novel antifungal protein with mitogenic activity from garland chrysanthemum seeds. 1150 60

Two novel antifungal peptides, designated alpha- and beta-basrubrins, respectively, were isolated from seeds of the Ceylon spinach Basella rubra. The purification procedure involved saline extraction, (NH(4))(2)SO(4) precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose and FPLC-gel filtration on Superdex peptide column. alpha- and beta-basrubrins exhibited a molecular weight of 4.3 and 5 kDa, respectively. They inhibited translation in a rabbit reticulocyte system with an IC(50) value of 400 and 100 nM, respectively. alpha- and beta-basrubrin inhibited HIV-1 reverse transcriptase by (79.4 +/- 7.8)% and (54.6 +/- 3.6)%, respectively, at a concentration of 400 microM, and (10.56 +/- 0.92)% and (2.12 +/- 0.81)%, respectively, at a concentration of 40 microM. Both alpha- and beta-basrubrins exerted potent antifungal activity toward Botrytis cinerea, Mycosphaerella arachidicola, and Fusarium oxysporum.
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PMID:Novel antifungal peptides from Ceylon spinach seeds. 1168 73

A deoxyribonuclease distinct from the previously isolated asparagus ribosome-inactivating proteins, possessing a molecular weight of 30 kDa and requiring a pH of 7.5 for optimum hydrolytic activity toward herring sperm DNA, was isolated from Asparagus officinalis seeds. The isolation procedure involved extraction with saline, (NH(4))(2)SO(4) precipitation, ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on CM-Sepharose, and FPLC gel filtration on Superdex 75. The doxyribonuclease was unadsorbed onto DEAE-cellulose and Affi-gel blue gel and adsorbed onto CM-Sepharose. It exhibited the novel N-terminal sequence, GIEVIKIREL. The deoxyribonuclease was purified to a specific activity of 1584 units/mg. It was devoid of ribonuclease, protease, and HIV-1 reverse transcriptase-inhibitory activities. However, it inhibited cell-free translation in a rabbit reticulocyte lysate system with an IC(50) of 20 microM. It exhibited antifungal activity toward Botrytis cinerea but not toward Fusarium oxysporum and Mycosphaerella arachidicola.
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PMID:Isolation of a novel deoxyribonuclease with antifungal activity from Asparagus officinalis seeds. 1170 87

A protease designated pleureryn, with an N-terminal sequence dissimilar from previously reported mushroom metalloendopeptidases and showing only limited resemblance to aspartic proteinases, albeit considerable homology to DNA replication licensing factor, was isolated from fresh fruiting bodies of the edible mushroom Pleurotus eryngii. The purification protocol entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel Blue gel, ion exchange chromatography on CM-Sepharose, and FPLC-gel filtration on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel Blue gel and CM-Sepharose. It demonstrated a single band with a molecular weight of 11.5 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Pleureryn demonstrated a protease activity of 9364 U/mg toward casein. It exhibited a pH optimum of 5.0 and a temperature optimum of 45 degrees C, with substantial activity remaining at high temperatures and pH 4 and 12. The activity of the protease was adversely affected by pepstatin A, indicating that it is an aspartic protease. PMSF, trypsin inhibitor, and EDTA exerted no striking effect, suggesting that it is neither a serine protease nor a metalloprotease. It inhibited translation in a rabbit reticulocyte lysate system with an IC(50) of 20 nM. Pleureryn also exhibited some inhibitory activity against HIV-1 reverse transcriptase, reminiscent of a suppressive action of HIV-1 protease on its homologous reverse transcriptase but was devoid of ribonuclease, deoxyribonuclease, and antifungal activities.
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PMID:Pleureryn, a novel protease from fresh fruiting bodies of the edible mushroom Pleurotus eryngii. 1172 12

A single-chained antifungal protein with a molecular weight of 6.5 kDa and displaying a novel N-terminal sequence was isolated from dried juvenile cicadas which are used in traditional Chinese medicine, by using ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose and then gel filtration on a Superdex peptide column. The peptide, designated cicadin, exerted potent antifungal activity with IC(50) values at nonomolar concentrations against a variety of fungi including Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum, Rhizoctonia solani and Coprinus comatus. Cicadin suppressed the activity of HIV-1 reverse transcriptase and stimulated the proliferation of murine splenocytes.
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PMID:Isolation of cicadin, a novel and potent antifungal peptide from dried juvenile cicadas. 1181 12

A ribosome inactivating peptide, with an N-terminal sequence exhibiting pronounced similarity to that of the 6.5 kDa-arginine/glutamate-rich polypeptide from Luffa cylindrica seeds, was isolated from seeds of a closely related species, the ridge gourd Luffa acutangula. The 5.6 kDa-peptide designated luffangulin inhibited cell-free translation with an IC50 of 3.5 nM but lacked inhibitory activity toward HIV-1 reverse transcriptase. It was similar to luffaculin, the 28 kDa ribosome inactivating protein in being unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel. On CM-cellulose luffangulin and luffaculin appeared as two adjacent peaks.
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PMID:Luffangulin, a novel ribosome inactivating peptide from ridge gourd (Luffa acutangula) seeds. 1185 28


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