Biomedical subjects

T B Ng

Publications and source records attributed to T B Ng.

At least 73 records · Page 4Linked to original sources

PubMed2004

A polymeric immunoglobulin receptor-like milk protein with inhibitory activity on human immunodeficiency virus type 1 reverse transcriptase.

A protein with a molecular mass of 85 kDa and an N-terminal sequence resembling polymeric immunoglobulin receptor has been isolated from bovine milk. The isolation procedure involved removal of globulin from acid whey by precipitation with 1.8 M (NH(4))(2)SO(4) followed by addition of (NH(4))(2)SO(4) to attain a concentration of 3.6 M. Subsequent steps included chromatography on CM-Sepharose and Mono S and elution of the protein of interest with a linear NaCl concentration gradient. The polymeric immunoglobulin receptor-like milk protein inhibited HIV-1 reverse transcriptase (RT) with an IC(50) of 4.8 microM. However, it did not exhibit ribonuclease activity. Neither did it inhibit translation in a cell-free rabbit reticulocyte lysate system.

Amino Acid Sequence↗

PubMed2004

The antioxidant effects of aqueous and organic extracts of Panax quinquefolium, Panax notoginseng, Codonopsis pilosula, Pseudostellaria heterophylla and Glehnia littoralis.

The roots of Panax quinquefolium, Panax notoginseng, Glehnia littoralis, Codonopsis pilosula and Pseudostellaria heterophylla were extracted with an aqueous extraction method and also with an organic extraction method. The aqueous extracts of Glehnia littoralis and Codonopsis pilosula were the most potent in inhibiting erythrocyte hemolysis. The aqueous extracts of Panax quinquefolium and Panax notoginseng had lower potencies while the aqueous extract of Pseudostellaria heterophylla and the organic extract of Panax quinquefolium were only weakly active. The organic extracts of Glehnia littoralis, Panax heterophylla and Panax quinquefolium were potent in inhibiting lipid peroxidation while the organic extracts of Codonopsis pilosula and Panax notoginseng had weaker potencies. The aqueous extracts possessed much lower potencies the corresponding organic extracts. However, the Glehnia littoralis extract was the most potent aqueous extract. The results suggest that Glehnia littoralis, Codonopsis pilosula, Panax notoginseng and Panax heterophylla are cheaper substitutes of Panax quinquefolium with regard to antioxidant activity.

Animals↗

PubMed2004

A ribonuclease from Chinese ginseng (Panax ginseng) flowers.

A ribonuclease, with a molecular mass of 23kDa, and much higher activity toward poly(U) than poly(C) and only negligible activity toward poly(A) and poly(G), was isolated from the aqueous extract of Chinese ginseng (Panax ginseng) flowers. The ribonuclease was unadsorbed on diethylaminoethyl-cellulose and adsorbed on Affi-gel blue gel and carboxymethyl-cellulose. High activity of the ribonuclease was maintained at pH 6-7. On either side of this pH range, there was a precipitous drop in enzyme activity. The activity of the enzyme peaked at 50 degrees C and fell to about 20% of the maximal activity when the temperature was lowered to 20 degrees C or raised to 80 degrees C. The characteristics of this ribonuclease were different from those of ribonuclease previously purified from ginseng roots.

Chromatography↗

PubMed2004

A ribonuclease with antimicrobial, antimitogenic and antiproliferative activities from the edible mushroom Pleurotus sajor-caju.

A 12 kDa ribonuclease preferential for poly U and with much lower activity toward poly A, poly G and poly C was isolated from fresh fruiting bodies of the mushroom Pleurotus sajor-caju. A purification procedure involving ion exchange chromatography on CM-cellulose, affinity chromatography on Red-Sepharose and Heparin-Sepharose, and fast protein liquid chromatography-gel filtration on Superdex 75 was used. The ribonuclease was adsorbed on all of the first three types of chromatographic media. It exhibited some activity toward herring sperm DNA and calf thymus DNA. The ribonuclease activity was unaffected in the presence of KCl (10 and 100 mM) and NaCl (100 mM and 1 M), but was strongly inhibited by CuSO4 (0.01 and 0.1 mM) and less potently inhibited by other divalent salts including MgCl2, CaCl2, ZnCl2, ZnSO4 and FeSO4. The optimal pH was 5.5 and the ribonuclease was stable up to 60 degrees C for 1 h. The ribonuclease inhibited mycelial growth in the fungi Fusarium oxysporum and Mycosphaerella arachidicola with an IC50 value of 95 and 72 microM, respectively. Out of the 12 species of bacteria tested, only Pseudomonas aeruginosa and Staphylococcus aureus were inhibited in growth by the ribonuclease. Viability of the tumor cells HepG2 (hepatoma) and L1210 (leukemia) was reduced with an IC50 of 0.22 and 0.1 microM, respectively in the presence of the ribonuclease. The ribonuclease inhibited translation in a cell-free rabbit reticulocyte lysate system with an IC50 of 158 nM and 3H-methyl-thymidine uptake by murine splenocytes with an IC50 of 65 nM.

Animals↗

PubMed2004

Isolation and characterization of a novel lectin from the wild mushroom Xerocomus spadiceus.

A lectin was isolated from extracts of fruiting bodies of the mushroom Xerocomus spadiceus using a procedure that involved 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 and Affi-gel blue gel and adsorbed on CM-Sepharose. The lectin was capable of eliciting an approximately four-fold stimulation of mitogenic response in murine splenocytes. The hemagglutinating activity was stable up to 60 degrees C, halved at 70 degrees C, reduced to 25% at 75 degrees C and dwindled to an undetectable level at 80 degrees C. The activity remained unaltered in the presence of various divalent (Ca2+, Mg2+, Zn2+ and Mn2+) chlorides up to a salt concentration of 10 mM except in the case of ZnCl2. FeCl3 up to a concentration of 10 mM did not affect the hemagglutinating activity of the lectin. The hemagglutinating activity of the lectin was doubled in the presence of 5 mM AlCl3 or 10 mM ZnCl2 and quadrupled in the presence of 10 mM AlCl3. The activity was reduced in the presence of HCl and NaOH. Among the large number of carbohydrates tested, only inulin was able to inhibit the hemagglutinating activity of the lectin.

Agaricales↗

PubMed2004

Eryngin, a novel antifungal peptide from fruiting bodies of the edible mushroom Pleurotus eryngii.

An antifungal peptide with a molecular mass of 10k Da was isolated from fruiting bodies of the mushroom Pleurotus eryngii. The peptide, designated as eryngin, inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola. It was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose. Its N-terminal sequence demonstrated some similarity to the antifungal protein from the mushroom Lyophyllum shimeiji and little resemblance to thaumatin and thaumatin-like proteins.

Antifungal Agents↗

PubMed2004

A napin-like polypeptide from dwarf Chinese white cabbage seeds with translation-inhibitory, trypsin-inhibitory, and antibacterial activities.

Napins are 1:1 disulfide-linked complexes of a smaller (ca. 4kDa) subunit and a larger (ca. 10kDa) subunit. The intent of the present study was to ascertain the production of napin by the seeds of a Brassica species that has not been examined previously, and also to explore new biological activities of the napin. A heterodimeric 11-kDa napin-like polypeptide has been isolated from Chinese white cabbage (Brassica chinensis cv dwarf) seeds with a protocol comprising ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, fast protein liquid chromatography (FPLC)-ion exchange chromatography on Mono S and FPLC-gel filtration on Superdex 75. The N-terminal sequence of the 7-kDa subunit manifests striking similarity to napin large chain, albumin and trypsin inhibitor. The N-terminal sequence of the 4-kDa subunit is homologous to napin large chain and an antimicrobial peptide. The napin-like polypeptide inhibited translation in the rabbit reticulocyte system with an IC50 of 18.5nM. This translation-inhibitory activity was stable between pH 4 and 11, and between 10 and 40 degrees C. The polypeptide inhibited trypsin with a higher potency ( IC50 = 8.5 microM) than it inhibited chymotrypsin (IC50 = 220 microM), but was devoid of ribonuclease and antifungal activities. It manifested antibacterial activity against Pseudomonas aeruginosia, Bacillus subtilis, Bacillus cereus, and Bacillus megaterium. The results revealed that the napin-like polypeptide from Chinese white cabbage seeds exhibited some potentially exploitable activities.

2S Albumins, Plant↗

PubMed2004

Multiple trypsin inhibitors from Momordica cochinchinensis seeds, the Chinese drug mubiezhi.

Five trypsin inhibitors, with N-terminal sequences demonstrating homology to each other and exhibiting a molecular weight of 5100, 4800, 4400, 4100, and 3900, respectively, were isolated from Momordica cochinchinensis seeds with a protocol involving acid extraction, ion exchange chromatography on SP-Sepharose chromatography, and RP-HPLC on a C18 column. Specific inhibitory activity against trypsin was demonstrated by the trypsin isoinhibitors with Ki values ranging from 5.3 x 10(-8) to 1.8 x 10(-6) M. None of the isoinhibitors could be cleaved by trypsin.

Amino Acid Sequence↗

PubMed2004

A new ribonuclease from the black oyster mushroom Pleurotus ostreatus.

A ribonuclease that is co-specific for poly C and poly U has been isolated from the fruiting bodies of the black oyster mushroom. The enzyme possesses a molecular mass of 14 kDa, and is unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and CM-cellulose. A pH of 7 is required for the enzyme to exhibit maximal activity. The activity of the enzyme does not vary appreciably over the temperature range 30-60 degrees C, but drops when the temperature is reduced to 20 degrees C or raised to and above 70 degrees C. The ribonuclease does not exert any inhibitory activity toward HIV-1 reverse transcriptase.

Chromatography, Liquid↗

PubMed2004

Adustin, a small translation-inhibiting polypeptide from fruiting bodies of the wild mushroom Polyporus adusta.

A polypeptide, with a molecular mass of 16.5 kDa as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, has been isolated from the mushroom Polyporus adusta. The polypeptide, designated as adustin, inhibited translation in a cell-free rabbit reticulocyte lysate system with an IC50 of 0.34 microM. It was isolated using a protocol that involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-Sepharose and fast protein liquid chromatography-gel filtration on Superdex 75. Adustin was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and CM-Sepharose.

Animals↗

PubMed2004

Alveolarin, a novel antifungal polypeptide from the wild mushroom Polyporus alveolaris.

An antifungal polypeptide, with a molecular mass of 28 kDa as judged by gel filtration and appearing as a single band with a molecular mass of 14 kDa in sodium dodecyl suflate-polyacrylamide gel electrophoresis, was isolated from fresh fruiting bodies of the mushroom Polyporus alveolaris. The antifungal polypeptide, designated as alveolarin, demonstrated an inhibitory action on mycelial growth in Botrytis cinerea, Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola. Alveolarin was isolated with a procedure that entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and gel filtration on Superdex 75 by fast protein liquid chromatography.

Antifungal Agents↗

PubMed2004

A novel ribonuclease from fruiting bodies of the common edible mushroom Pleurotus eryngii.

A ribonuclease with a temperature optimum of about 70 degrees C and a pH optimum of 6.5 was isolated from fruiting bodies of the mushroom Pleurotus eryngii. The ribonuclease was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose. It possessed a molecular mass of 16 kDa, and exhibited higher ribonucleolytic activity toward poly A and poly G and lower ribonucleolytic activity toward poly C and poly U. Its N-terminal sequence was distinctly different from those of other mushroom ribonucleases, and resembled that of Pleurotus tuber-regium only by 40%. Furthermore, its thermostability characteristics, polyhomoribonucleotide specificity and molecular mass were dissimilar to those of other mushroom ribonucleases.

Amino Acid Sequence↗

PubMed2004

Flammin and velin: new ribosome inactivating polypeptides from the mushroom Flammulina velutipes.

A protein designated flammin and exhibiting a molecular mass of 30kDa, and another protein designated velin and possessing a molecular mass of 19 kDa, were isolated from the fruiting bodies of the edible mushroom Flammulina velutipes. Flammin and velin inhibited translation in a rabbit reticulocyte lysate system with an IC(50) of 1.4 and 2.5 nM, respectively. Flammin demonstrated only a small degree of resemblance in N-terminal sequence to angiosperm type 1 ribosome inactivating proteins (RIPs) such as trichosanthin, alpha-momorcharin and beta-momorcharin but no sequence similarity to other mushroom RIPs. Velin manifested limited sequence homology to the A chain of abrin, a type 2 angiosperm RIP. Neither flammin nor velin showed any ribonuclease or protease activity. Both flammin and velin were unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and CM-Sepharose. They were separable in gel filtration on Superdex 75 by fast protein liquid chromatography.

Agaricales↗

PubMed2004

Isolation of a new ribonuclease from fruiting bodies of the silver plate mushroom Clitocybe maxima.

A ribonuclease, with an N-terminal sequence exhibiting some homology to ribonuclease from Pleurotus ostreatus (Family Pleurotaceae), has been purified from fruiting bodies of the silver plate mushroom Clitocybe maxima (Family Tricholomataceae). However, there is little resemblance between the N-terminal sequences of ribonucleases from various Pleurotus species, and a lesser extent of resemblance between ribonucleases from C. maxima and Pleurotus tuber-regium. No structural relationship exists between ribonuclease from C. maxima, and those from Volvariella volvacea, Lentinus edodes and Irpex lacteus. The purification protocol involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-Sepharose, and fast protein liquid chromatography on Superdex 75. The ribonuclease was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and CM-Sepharose. It exhibited a molecular mass of 17.5 kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It manifested roughly the same ribonucleolytic potency toward poly A and poly G followed by poly U. Its activity toward poly C was, by comparison, meager. The temperature and pH required for its optimal activity were, respectively, 70 degrees C and 6.5-7.0.

Agaricales↗

PubMed2004

Antifungal proteins and peptides of leguminous and non-leguminous origins.

Antifungal proteins and peptides, as their names imply, serve a protective function against fungal invasion. They are produced by a multitude of organisms including leguminous flowering plants, non-leguminous flowering plants, gymnosperms, fungi, bacteria, insects and mammals. The intent of the present review is to focus on the structural and functional characteristics of leguminous, as well as non-leguminous, antifungal proteins and peptides. A spectacular diversity of amino acid sequences has been reported. Some of the antifungal proteins and peptides are classified, based on their structures and/or functions, into groups including chitinases, glucanases, thaumatin-like proteins, thionins, and cyclophilin-like proteins. Some of the well-known proteins such as lectins, ribosome inactivating proteins, ribonucleases, deoxyribonucleases, peroxidases, and protease inhibitors exhibit antifungal activity. Different antifungal proteins may demonstrate different fungal specificities. The mechanisms of antifungal action of only some antifungal proteins including thaumatin-like proteins and chitinases have been elucidated.

Amino Acid Sequence↗

PubMed2004

Peptides and proteins from fungi.

The peptides and proteins secreted by fungi are reviewed in this article. They include ribosome inactivating peptides and proteins, antifungal peptides and proteins, lectins, ubiquitin-like peptides and proteins, peptides and proteins with nucleolytic activity, proteases, xylanases, cellulases, sugar oxidoreductases, laccases, invertases, trehalose phosphorylases, and various enzymes with applications in food industry, chemical production and the medical sector.

Fungal Proteins↗

PubMed2004

Actinchinin, a novel antifungal protein from the gold kiwi fruit.

An antifungal protein designated actinchinin, with an N-terminal sequence different from that of the thaumatin-like antifungal protein from green kiwi fruit, was isolated from the gold kiwi fruit. The antifungal protein, unlike its counterpart from green kiwi fruit, did not exert antifungal activity against Botrytis cinerea, but was active against Fusarium oxysporum which was unresponsive to thaumatin-like protein from green kiwi fruit. Actinchinin was isolated using a protocol that comprised ion exchange chromatography on CM-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on Superdex 75. Actinchinin was adsorbed on CM-cellulose, Affi-gel blue gel and Mono S. It was devoid of mitogenic activity toward mouse splenocytes. In contrast to thaumatin-like protein from green kiwi fruit, actinchinin lacked HIV-1 reverse transcriptase inhibiting activity.

Actinidia↗

PubMed2004

A non-specific lipid transfer protein with antifungal and antibacterial activities from the mung bean.

A non-specific lipid transfer peptide (nsLTP) with antimicrobial activity was isolated from the mung bean (Phaseolus mungo) seeds. The procedure entailed aqueous extraction, ion exchange chromatography on CM-Sephadex and high performance liquid chromatography (HPLC) on POROS-HS-20. The peptide exhibited a molecular mass of 9.03 kDa in mass spectrometry. It exerted antifungal action toward Fusarium solani, Fusarium oxysporum, Pythium aphanidermatum and Sclerotium rolfsii, and antibacterial action against Staphylococcus aureus but not against Salmonella typhimurium. The lipid binding of this peptide was very similar to that of a previously described lipid transfer protein extracted from wheat seeds and maize seeds, indicating that it possessed lipid transfer activity. The present findings add to the scarcity of the literature on leguminous nsLTPs.

Anti-Bacterial Agents↗