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Articles by M. Habibur Rahman
Total Records ( 3 ) for M. Habibur Rahman
  M. Habibur Rahman , M. Badrul Alam , N.S. Chowdhury , M.K. Jha , M. Hasan , M.M. Khan , M.S. Rahman and M. Ekramul Haque
  In the present study crude methanolic extract of Stephania japonica leaf was investigated for possible antioxidant, analgesic and toxic activity. The extract showed antioxidant activity in DPPH radical scavenging activity, nitric oxide scavenging activity and reducing power assays. In both DPPH radical and NO scavenging assay, the extract exhibited moderate antioxidant activity and the IC50 values in DPPH radical scavenging and NO scavenging assays were found to be 105.55±1.06 and 129.12±0.15 μg mL-1, respectively while the IC50 values of ascorbic acid were 12.30±0.11 and 18.64±0.22 μg mL-1, respectively. Reducing power activity of the extract increased in a dose dependent manner. Analgesic activity of the crude extract was evaluated using acetic acid-induced writhing model of pain in mice. The crude extract at 200 and 400 mg kg-1 b.wt. doses displayed significant (p<0.001) reduction in acetic acid induced writhing in mice with a maximum effect of 75.89% reduction at 400 mg kg-1 b.wt. which is comparable to the standard, diclofenac sodium (86.52%). The extract was also investigated for toxic potentiality using Brine Shrimp lethality bioassay. In this bioassay the extract showed significant toxicity to Brine Shrimp nauplii with the LC50 value of 25.19±0.98 μg mL-1. The study clearly indicates that the extract possesses good analgesic and cytotoxic activity along with moderate antioxidant potential.
  M. Habibur Rahman , A. S. M. Aynul Haque Akand , Tanzima Yeasmin , Md. Salim Uddin and Mahbubur Rahman
  A mango invertase was purified from the flesh of Himsagar variety to an electrophoretically homogeneous state, by successive ion-exchange chromatography on DEAE-Cellulose and CM-Cellulose column chromatography. The molecular weight of the purified enzyme was 68 kDa in gel filtration chromatography and 65.5 kDa on SDS-polyacrylamide gel electrophoresis. However, SDS-polyacrylamide gel electrophoresis revealed four bands, indicating that the enzyme was a tetramer. The enzyme was a glycoprotein as it gave yellow-orange colour in the presence of phenol sulphuric acid. The optimum pH for the enzyme was 4.5 and the enzyme was found to be stable from pH 2.5 to 8. The optimum temperature for enzyme was 75°C and the enzyme was stable between 10 - 75°C. The Km for sucrose was 5.25 mM (pH 4.5). The activities of enzyme were remarkably enhanced by Cu++, K+, Ca++ whereas, completely ceased by Hg++ and sodium dodecylsulfate.
  M. Habibur Rahman and Mikiko Ikeda
  Three cDNAs (named pVC1, pVC2 and pVC3) have been isolated from a giant alga, Acetabularia acetabulum that encoded the N, N´- icyclohexylcarbodimide-binding 16 kDa proteolipid subunit of V-ATPase. The open reading frames of pVC1, pVC2 and pVC3 predicted the polypeptides of 164, 167 and 168 amino acids with the molecular masses of 16.5, 16.7 and 16.8 kDa, respectively. Seventy nine percent identity between pVC1 and pVC2 or pVC3 and 95% identity between pVC2 and pVC3 was observed. PVC1 and pVC2/pVC3 showed extensive divergences in their 3´ -untranslated region, while pVC2 and pVC3 possessed the same 3´ -untranslated region. The deduced amino acid sequences of the three cDNA clones showed extensive similarities with that of proteolipids of oat (75 to 80%), bovine (55%) and yeast (55%) V-ATPase. Based on hydropathy plot, four membrane-spanning domains were predicted, in which domain IV was especially conserved among different species. This domain showed 96-100% identity in amino acid sequences between the A. acetabulum and the oat proteolipid in which a glutamate residue is included, the putative N, N´-dicyclohexylcarbodimide-binding residue.
 
 
 
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