Mangifera indica showed highest percentage (100%) of mycorrhizal colonization in Rajshahi Univers... more Mangifera indica showed highest percentage (100%) of mycorrhizal colonization in Rajshahi University Campus, Bangladesh that was used as a stock plant in pot culture experiment. These root pieces have the ability to serve as a source of mycorrhizal inoculum for crop plants. ...
A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity... more A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity chromatography on ConA Sepharose. The lectin is monomer in nature as judged by SDS-PAGE and its MW was estimated to be 22,000. The lectin is glycoprotein with neutral sugar content of 28.57%, and mannose and glucose were identified as carbohydrate. The lectin agglutinated rat red blood cells and in a hapten inhibition test, D-mannose and D-glucose was found to be inhibitor. The lectin also exhibited cytotoxic effect in brine shrimp lethality bioassay. The N-terminal sequences of the lectin upto 45-residues except the positions of 21, 39, 42 and 44 were identified. Sequence homology of the lectin is also discussed.
An intracellular protease was extracted and purified from Pseudomonas aeruginosa by ion-exchange ... more An intracellular protease was extracted and purified from Pseudomonas aeruginosa by ion-exchange chromatography on DEAE-cellulose followed by CM-cellulose and rechromatography on DEAE-cellulose. The purified protease was found to be homogeneous as judged by polyacrylamide disc gel electrophoresis (PAGE). The molecular mass of the protease as determined by gel filtration on G-150 was about 48,000 and about 49,000 on SDS-PAGE. The enzyme is monomeric in nature. The purified protease is a glycoprotein with neutral sugar content of 0.6%. The Km value of the protease was found to be 0.48% against casein as substrate. The enzyme is stable up to 60 0 C and showed maximum activity around 50 0 C. The enzyme activity was affected with the changes of pH and the maximum proteolytic activity was observed at pH 8.0. The protease activity was inhibited in the presence of EDTA, Cu 2+ , Mn 2+ and Hg 2+ whereas the presence of Ca 2+ , K + , Na + and ascorbic acid enhanced the activity.
Mangifera indica showed highest percentage (100%) of mycorrhizal colonization in Rajshahi Univers... more Mangifera indica showed highest percentage (100%) of mycorrhizal colonization in Rajshahi University Campus, Bangladesh that was used as a stock plant in pot culture experiment. These root pieces have the ability to serve as a source of mycorrhizal inoculum for crop plants. ...
A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity... more A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity chromatography on ConA Sepharose. The lectin is monomer in nature as judged by SDS-PAGE and its MW was estimated to be 22,000. The lectin is glycoprotein with neutral sugar content of 28.57%, and mannose and glucose were identified as carbohydrate. The lectin agglutinated rat red blood cells and in a hapten inhibition test, D-mannose and D-glucose was found to be inhibitor. The lectin also exhibited cytotoxic effect in brine shrimp lethality bioassay. The N-terminal sequences of the lectin upto 45-residues except the positions of 21, 39, 42 and 44 were identified. Sequence homology of the lectin is also discussed.
An intracellular protease was extracted and purified from Pseudomonas aeruginosa by ion-exchange ... more An intracellular protease was extracted and purified from Pseudomonas aeruginosa by ion-exchange chromatography on DEAE-cellulose followed by CM-cellulose and rechromatography on DEAE-cellulose. The purified protease was found to be homogeneous as judged by polyacrylamide disc gel electrophoresis (PAGE). The molecular mass of the protease as determined by gel filtration on G-150 was about 48,000 and about 49,000 on SDS-PAGE. The enzyme is monomeric in nature. The purified protease is a glycoprotein with neutral sugar content of 0.6%. The Km value of the protease was found to be 0.48% against casein as substrate. The enzyme is stable up to 60 0 C and showed maximum activity around 50 0 C. The enzyme activity was affected with the changes of pH and the maximum proteolytic activity was observed at pH 8.0. The protease activity was inhibited in the presence of EDTA, Cu 2+ , Mn 2+ and Hg 2+ whereas the presence of Ca 2+ , K + , Na + and ascorbic acid enhanced the activity.
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