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Articles by Nurul Absar
Total Records ( 5 ) for Nurul Absar
  Anwarul Islam , Abu Sayeed , Nurul Absar and Md. Ibrahim H. Mondal
  An experiment was conducted to find out the enzymatic change in jute leaves under different foliar treatments in the experimental land of the Institute of Biological Sciences, Rajshahi University during the period of April-May, 2000-2001. The effect of NPK-fertilizers and cowdung as well as foliar spray of urea and chemicals on the changes in the enzyme contents of matured jute leaves was analyzed. It was found that the activities of all the experimental enzymes in the leaves from treated jute plants were increased significantly as compared to those in control ones. Of the enzymes examined, the activities of protease were found to be increased highest (93.33%), followed by cellulase (88.57%), invertase (87.50%) and so on in decreasing order.
  Anwarul Islam , Abu Sayeed , Nurul Absar , Md. Ibrahim H. Mondal and Shamsul Alam
  The experiment was performed in the experimental land of the Institute of Biological Sciences, Rajshahi during the period of April-May, 2000 and 2001. The physicochemical compositions of jute leaves under different foliar treatments were investigated at the mature stage. The results obtained showed significantly increase in most of the chemical composition under different treatments. The soil of the cultivated land as well as jute leaves obtained from experimental land became less acidic as compared to those of control field after application of NPK-fertilizers and cowdung in combination with foliar spray. The highest percentage of increase of jute plant and physico-chemical composition of leaves as compared to those of control were as follows: length of jute plant 38.35%, area of jute leaf 160.00%, specific gravity 6.48%, dry matter 27.78%, ash content 18.55%, total chlorophyll 42.17%, total sugar 69.47%, reducing sugar 48.15%, non-reducing sugar 72.90%. Only the moisture content of jute leaves from control jute plant was about to higher as compared to that from experimental jute leaves.
  M. Abbas Ali , M. Abu Sayeed and Nurul Absar
  Three lectins CSL-1, CSL-2 and CSL-3, purified from the Cassia fistula seeds were tested for their antibacterial activities against 14 pathogenic bacteria using 30 μg/disc. The lectin CSL-3 was found to be active against all of the bacterial strains and showed strong activity against Bacillus megaterium, Streptococcus β-haemolyticus and Shigella boydii. The lectin CSL-2 showed poor activity against most of the bacterial strains and has strong activity against only Streptococcus β-haemolyticus. But the lectin CSL-1 was found to be inactive against all the bacterial strains except Streptococcus β-haemolyticus and Sarcina lutea. All the lectins affect significantly the mortality rate of brine shrimp. Among them CSL-2 was found to be highly toxic (6.68 μg ml-1) followed by CSL-1 (10.47 μg ml-1) and then CSL-3 (13.33 μg ml-1).
  Shahanaz Khatun , Nurul Absar and M. Ashraduzzaman
  Polyphenoloxidase (PPO), a highly active oxidative enzyme in Sajna leaves at mature stage was purified by ion exchange chromatography on DEAE-cellulose followed by CM-cellulose. The purified enzyme was monomer in nature and its molecular weight was estimated to be 56,000 and 55,500 by gelfiltration and SDS-PAGE respectively. The enzyme appeared to be a single polypeptide chain as revealed by SDS-PAGE either in presence or absence of reducing agent. The enzyme has following characteristics : optimum pH 6.2, optimum temperature 32°C, Km value 0.047M against catechol as substrate and maximum absorption 279 nm. The activity of the enzyme was enhanced by Ca2+ and Cu2+ but its activity lost completely in presence of ascorbic acid, EDTA, KCN and NaHSO3.
  Syed Rashel Kabir , Syed Enamul Hossain and Nurul Absar
  Two lectins from the rice bran of Amon variety were purified by successive chromatography of 100% ammonium sulfate saturated crude extract on Sephadex G-50 followed by ion-exchange chromatography on DEAE-cellulose. Both the lectins are found to be homogenous as judged by polyacrylamide gel electrophoresis. The molecular weight of the lectins, RBL-1 and RBL-2 as determined by gel filtration and SDS-PAGE were estimated to be as 22,000 and 36,000 respectively. The lectins are dimer and their subunits are held together by disulfide bonds. The lectins agglutinated rat red blood cells and the agglutination was inhibited specifically by D-glucose, D (+) glucosamine-HCl and N-acetyl-D-glucosamine. The lectins are glycoprotein in nature with neutral sugar content of 4 - 5.4%. The lectins RBL-2 are more cytotoxic than RBL-1 as observed by brine shrimp nauplii mortality rate bioassay.
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