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Affi-gel Blue Gel (affi-gel + blue_gel)
Selected AbstractsA Thermostable Chitinase with Chitin-Binding Activity from Phaseolus limensisJOURNAL OF FOOD SCIENCE, Issue 6 2008S.Y. Wang ABSTRACT:, A 28.6-kDa chitinase with chitin-binding activity was isolated from the large lima bean (Phaseolus limensis) seeds. The procedure entailed extraction, ammonium sulfate precipitation, affinity chromatography on Affi-gel blue gel, and high-performance liquid chromatography (HPLC) on SP-Toyopearl. There was an almost 108-fold increase in specific activity of the purified chitinase compared with that of the crude extract. The enzyme exhibited a pI of 7.8 by isoelectric focusing electrophoresis. The optimum pH and the optimum temperature for activity toward N-acetyld-glucosamine were 5.4 and 40 to 50 °C, respectively. The enzyme was stable up to 55 °C. It exerted a potent inhibitory action toward fungal species, including Fusarium solani, Pythium aphanidermatum, and Sclerotium rolfsii. [source] A new peptidic protease inhibitor from Vicia faba seeds exhibits antifungal, HIV-1 reverse transcriptase inhibiting and mitogenic activitiesJOURNAL OF PEPTIDE SCIENCE, Issue 12 2002X. Y. Ye Abstract A new trypsin,chymotrypsin inhibitor, with an N -terminal sequence showing some differences from the previously reported trypsin,chymotrypsin inhibitor, was isolated from the broad bean Vicia faba. The inhibitor was a peptide with a molecular mass of 13 kDa. It was adsorbed on Affi-gel blue gel and CM-Sepharose. It exerted antifungal activity toward Mycosphaerella arachidicola and Physalospora piricola. In addition, the trypsin,chymotrypsin inhibitor elicited a mitogenic response from mouse splenocytes and inhibited the activity of human immunodeficiency virus-1 reverse transcriptase. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd. [source] Purification of Angularin, A Novel Antifungal Peptide from Adzuki BeansJOURNAL OF PEPTIDE SCIENCE, Issue 3 2002Dr X. Y. Ye Abstract An antifungal peptide was isolated from the adzuki bean with a procedure involving affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The protein designated angularin was adsorbed on both types of chromatographic media and possessed a molecular weight of 8 kDa. Angularin exhibited antifungal activity against a variety of fungal species including Mycospharella arachidiocola and Botrytis cinerea. It inhibited mycelial growth in B. cinerea with an IC50 of 14.3 µM. Fusarium oxysporum and Rhizoctonia solani were not inhibited. Angularin demonstrated inhibitory activity on translation in the rabbit reticulocyte lysate system (IC50 = 8.0 µM) but did not affect proliferation of splenocytes. The activity of HIV-1 reverse transcriptase was inhibited in the presence of angularin. Its N -terminal sequence was GEPGQKE. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd. [source] Characterisation of a haemagglutinin from Hokkaido red bean (Phaseolus vulgaris cv. Hokkaido red bean)JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 1 2010Jack H Wong Abstract BACKGROUND: A haemagglutinin was purified from Japanese Hokkaido red beans (Phaseolus vulgaris cv. Hokkaido red bean) with a procedure that included three chromatographic media. RESULTS: Haemagglutinating activity was adsorbed on DEAE cellulose, Affi-gel blue gel and Mono S. The pure haemagglutinin was a homodimer and each subunit was around 30 kDa in molecular mass. The haemagglutinating activity of this agglutinin could not be inhibited by a variety of simple sugars at 200 mmol L,1 concentration including ,- L -fucose, D(+)-galactose, D(+)-glucose, D(+)-glucosamine, D(,)galactosamine, galacturonic acid, (+)-lactose, D(+)-melibose, L(,)-mannose, D(+)-mannose, D -mannosamine, D(+)-raffinose, L -rhamnose, (+)-xylose and galacturonic acid. The haemagglutinating activity was fully retained at pH 4,11 and at 0,80 °C, but was completely lost at extreme pH values (0,2 and 13,14) and at very high temperatures (90 °C and 100 °C). The haemagglutinin exhibited a weak mitogenic activity toward mouse splenocytes, a stronger anti-proliferative activity than Con A toward HepG2 (human hepatoma) cells and inhibited >80% of HIV-1 reverse transcriptase inhibitory activity at 3.3 µmol L,1. It was devoid of anti-fungal activity. CONCLUSION: Hokkaido red bean haemagglutinin possesses a potent anti-proliferative effect on HepG2 cells. Copyright © 2009 Society of Chemical Industry [source] A low-molecular mass ribonuclease from the brown oyster mushroomCHEMICAL BIOLOGY & DRUG DESIGN, Issue 1 2005L. Xia Abstract:, A ribonuclease, with a molecular mass of 9 kDa and an N-terminal sequence resembling the sequence of a fragment of tRNA/rRNA cytosine-C5-methylase and a fragment of a alanyl-tRNA synthetase, was isolated from fresh fruiting bodies of the brown oyster mushroom Pleurotus ostreatus. The ribonuclease was purified using a very simple protocol that comprised ion-exchange chromatography on carboxymethyl (CM)-cellulose and affinity chromatography on Affi-gel blue gel. Subsequent gel filtration by fast protein liquid chromatography on Superdex 75 and sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis revealed that the ribonuclease was purified after the first two chromatographic steps. The ribonuclease was adsorbed on CM-cellulose and Affi-gel blue gel. The ribonuclease exhibited the highest activity toward poly A, lower activity toward poly C, slight activity toward poly G, and indiscernible activity toward poly U. The enzyme was stimulated upon exposure to 1 ,m Mg2+ and 10 ,m Zn2+, but was inhibited by the following ions at 10 mm: Ca2+, Mg2+, Zn2+, Cu2+, Fe2+, Mn2+, and Fe3+. The ribonuclease required a pH of 8.0 and a temperature of 50,70 °C to express maximal activity. It had a Km of 60 ,m toward yeast tRNA. It lacked mitogenic and HIV-1 reverse transcriptase inhibiting activities, but exerted antiproliferative activity toward leukemia L1210 cells. [source] | ||||||||||